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Prion Protein Found in Skin of CJD Patients

Dark green areas are countries that have confirmed human cases of variant Creutzfeldt-Jakob disease and light green are countries that have bovine spongiform encephalopathy cases. Graphic credit: CC BY-SA 3.0,

Funding for this project was provided by the NIH/National Institute of Allergy and Infectious Diseases


Transmissible spongiform encephalopathy diseases are caused by prions. Prions are proteins that occur normally in neurons of the central nervous system (CNS). These proteins are thought to affect signaling processes, damaging neurons and resulting in degeneration that causes the spongiform appearance in the affected 1) ___. The CJD prion is dangerous because it promotes refolding of native prion protein into the diseased state. The number of misfolded protein molecules will increase exponentially and the process leads to a large quantity of insoluble protein in affected cells. This mass of misfolded proteins disrupts neuronal cell function and causes cell 2) ___. Mutations in the gene for the prion protein can cause a misfolding of the dominantly alpha helical regions into beta pleated sheets. This change in conformation disables the ability of the protein to undergo digestion. Once the prion is transmitted, the defective proteins invade the brain and induce other prion protein molecules to misfold in a self-sustaining feedback loop. These neurodegenerative diseases are commonly called prion diseases.


People can also develop CJD because they carry a mutation of the gene that codes for the prion protein (PRNP). This occurs in only 5-10% of all CJD cases. In sporadic cases the misfolding of the prion 3) ___ probably occurs as a natural, spontaneous process. An EU study determined that “87% of cases were sporadic, 8% genetic, 5% iatrogenic and less than 1% variant.“


National Institutes of Health (NIH) scientists and collaborators at Case Western Reserve University School of Medicine have detected abnormal prion protein in the skin of nearly two dozen people who died from Creutzfeldt-Jakob disease (CJD). The scientists also exposed a dozen healthy mice to skin extracts from two of the CJD patients, and all developed prion disease. The study results, published in Science Translational Medicine, raise questions about the possible transmissibility of prion diseases via medical procedures involving skin, and whether 4) ___ samples might be used to detect prion disease. Researchers from NIH’s National Institute of Allergy and Infectious Diseases (NIAID) were co-leaders of the study, which included multiple collaborating groups. They stress that the prion-seeding potential found in skin tissue is significantly less than what they have found in studies using brain tissue.


CJD is an incurable — and ultimately fatal — transmissible, neurodegenerative disorder in the family of prion diseases. Prion diseases originate when normally harmless prion protein molecules become abnormal and gather in clusters and filaments in the human body and brain. The reasons for this process are not fully understood. The accumulation of these clusters has been associated with tissue damage that leaves sponge-like holes in the brain. Human prion diseases include fatal insomnia; kuru; Gerstmann-Straussler-Scheinker syndrome; and variant, familial and sporadic CJD. Sporadic CJD is the most common human prion disease, affecting about one in one million people annually worldwide. Other 5) ___ diseases include scrapie in sheep; chronic wasting disease in deer, elk and moose; and bovine spongiform encephalopathy, or mad cow disease, in cattle. Most people associate prion diseases with the brain, although scientists have found abnormal infectious prion protein in other organs, including the spleen, kidney, lungs and liver. Sporadic CJD is known to be transmissible by invasive medical procedures involving the central 6) ___system and cornea, but transmission via skin had not been a common concern.


Using a test for prion diseases known as Real-Time Quaking-Induced Conversion (RT-QuIC), scientists analyzed skin tissue from 38 patients — 23 who had died from CJD, and 15 who died of other causes. They also collected brain tissue from the 23 CJD patients and from seven individuals who died of other causes. RT-QuIC correctly detected abnormal prion protein in each CJD patient sample tested and in none of the non-CJD group. The scientists noted that in the CJD group, the “seeding potential“ for normal prion protein to convert to abnormal was 1,000 to 100,000 times lower in skin than brain 7) ___. The scientists then exposed humanized laboratory mice to either brain or skin extracts from two of the CJD patients. All 12 mice inoculated with brain tissue developed prion disease, as did all 12 inoculated with skin extracts, though disease in the skin group took about twice as long — roughly 400 days — to develop. The group also reported that brain degeneration in both groups of infected 8) ___ was similar. The study authors say the results should generate discussion about potential surgical instrument contamination and risk associated with procedures involving CJD patients. “Perspective is important when interpreting these outcomes,“ said Byron Caughey, Ph.D., a senior investigator at NIAID’s Rocky Mountain Laboratories (RML) who helped oversee the study. “This study used humanized mice with tissue extracts directly inoculated into the brain, so the system was highly primed for infection. There is no 9) ___ that transmission can occur in real-world situations via casual skin contact. However, the results raise transmission questions that warrant further study.“ The study also raises the possibility of using RT-QuIC with skin tissue samples as a diagnostic test for human and animal prion diseases. The test is widely used with samples of brain and spinal-fluid for the diagnosis of CJD, but such samples are not always available. “Our objective has always been to facilitate RT-QuIC testing using the most broadly available and least-invasive sample possible, whether that is blood, skin, nasal brushings, or other samples,“ Dr. Caughey said. His research group has developed RT-QuIC over the past decade at RML, where he also has trained many international colleagues to use and advance the 10) ___. Dr. Caughey’s group is continuing its development of RT-QuIC applications, including further studies of when and where the pathological prion protein appears in skin, and how to effectively inactivate its infectious forms. Sources: NIH/National Institute of Allergy and Infectious Diseases; ScienceDaily; Wikipedia; Prion seeding activity and infectivity in skin samples from patients with sporadic Creutzfeldt-Jakob disease. Science Translational Medicine, 2017; 9 (417): eaam7785 DOI: 10.1126/scitranslmed.aam7785


ANSWERS: 1) brain; 2) death; 3) protein; 4) skin; 5) prion; 6) nervous; 7) tissue; 8) mice; 9) evidence; 10) test


Hans Gerhard Creutzfeldt MD

Hans Gerhard Creutzfeldt (June 2, 1885 – December 30, 1964) was a German neuropathologist, who first described the Creutzfeldt-Jakob disease. He was born in Harburg upon Elbe and died in Munich.

Photo credit: Unknown –, Public Domain,



Hans Gerhard Creutzfeldt was born into a medical family in Harburg, which was incorporated into Hamburg in 1937. In 1903, at the age of 18, Creutzfeldt was drafted into the German army and spent his service stationed in Kiel. Afterwards, he attended the School of Medicine of the Universities of University of Jena and University of Rostock, receiving his doctorate at the latter in 1909. Part of his practical training was undertaken at St. Georg – Hospital in Hamburg. After qualification he sought adventure as a ship’s surgeon, voyaging the Pacific Ocean, taking the opportunity to study local crafts, linguistics, and tropical plants. After returning to Germany, Creutzfeldt worked at the Neurological Institute in Frankfurt am Main, at the psychiatric-neurological clinics in Breslau, Kiel and Berlin, and at the Deutsche Forschungsanstalt fur Psychiatrie in Munich. Creutzfeldt was habilitated at Kiel in 1920, and in 1925 became Extraordinarius of psychiatry and neurology. In 1938 he was appointed professor and director of the university psychiatric and neurological division in Kiel. Later, Creutzfeldt helped to recognize a neurodegenerative disease, with Alfons Maria Jakob, now known as Creutzfeldt-Jakob disease, in which the brain tissue develops holes and takes on a sponge-like texture. It is now known that this disease is due to a type of infectious protein called a prion. Prions are misfolded proteins which replicate by converting their properly folded counterparts.


In the Third Reich, Creutzfeldt became a Patron Member of Heinrich Himmler’s SS. However, when Creutzfeldt was 54 years old and WW2 broke out, he was unmoved by the Nazi regime and was able to save some people from death in concentration camps. He also managed to rescue almost all of his patients from being murdered under the Nazi Action T4 euthanasia program, an unusual event since most mental patients identified by T4 personnel were gassed or poisoned at separate euthanasia clinics such as Hadamar Euthanasia Centre. During the war, bombing raids destroyed his home and clinic. After the war he was director of the University of Kiel for six months, before being dismissed by the British occupation forces. His efforts to rebuild the university caused a series of conflicts with the British because he wanted to allow more former army officers to study there. In 1953 he moved on to Munich to work on scientific research commissioned by the Max Planck Society.


Creutzfeldt was married to Clara Sombart, a daughter of Werner Sombart. They had five children, among them Otto Detlev Creutzfeldt and Werner Creutzfeldt (1924-2006), a renowned German Internist. Hans Gerhard Creutzfeldt died in 1964 in Munich.


As mentioned above, Creutzfeldt-Jakob disease, is a subacute spongiform encephalopathy caused from prions involving the cerebral cortex, the basal ganglia and the spinal cord. Some of the clinical findings described in the Creutzfeldt and Jakob first papers do not match current criteria for Creutzfeldt-Jakob disease. It has been speculated that at least two of the patients in initial studies were suffering from a different ailment. A study published in 1997 counted more than 100 cases worldwide of transmissible CJD and new cases continued to appear at the time. The first report of suspected iatrogenic CJD was published in 1974. Animal experiments showed that corneas of infected animals could transmit CJD, and the causative agent spreads along visual pathways. A second case of CJD associated with a corneal transplant was reported without details. In 1977, CJD transmission caused by silver electrodes previously used in the brain of a person with CJD was first reported. Transmission occurred despite decontamination of the electrodes with ethanol and formaldehyde. Retrospective studies identified four other cases likely of similar cause. The rate of transmission from a single contaminated instrument is unknown, although it is not 100%. In some cases, the exposure occurred weeks after the instruments were used on a person with CJD.


A review article published in 1979 indicated that 25 dura mater cases had occurred by that date in Australia, Canada, Germany, Italy, Japan, New Zealand, Spain, the United Kingdom, and the United States.

By 1985, a series of case reports in the United States showed that when injected, cadaver-extracted pituitary human growth hormone could transmit CJD to humans. In 1992, it was recognized that human gonadotropin administered by injection could also transmit CJD from person to person. In 2004, a report published by Edinburgh doctors in the Lancet medical journal demonstrated that vCJD was transmitted by blood transfusion.


Stanley B. Prusiner of the University of California, San Francisco (UCSF) was awarded the Nobel Prize in physiology or medicine in 1997 “for his discovery of Prions – a new biological principle of infection“. However, Yale University neuropathologist Laura Manuelidis has challenged the prion protein (PrP) explanation for the disease. In January 2007, she and her colleagues reported that they had found a virus-like particle in naturally and experimentally infected animals. “The high infectivity of comparable, isolated virus-like particles that show no intrinsic PrP by antibody labeling, combined with their loss of infectivity when nucleic acid-protein complexes are disrupted, make it likely that these 25-nm particles are the causal TSE virions.“ Four Australians had been reported with CJD following transfusion as of 1997. There have been ten cases of healthcare-acquired CJD in Australia. They consist of five deaths following treatment with pituitary extract hormone for either infertility or short stature, with no further cases since 1991. The five other deaths were caused by dura grafting during brain surgery, where the covering of the brain was repaired. There have been no other known healthcare-acquired CJD deaths in Australia. A case was reported in 1989 in a 25-year-old man from New Zealand, who also received dura mater transplant. Five New Zealanders have been confirmed to have died of the sporadic form of Creutzfeldt-Jakob disease (CJD) in 2012.


Researchers believe one in 2,000 people in the UK is a carrier of the disease linked to eating contaminated beef (vCJD). The survey provides the most robust prevalence measure to date – and identifies abnormal prion protein across a wider age group than found previously and in all genotypes, indicating “infection“ may be relatively common. This new study examined over 32,000 anonymous appendix samples. Of these, 16 samples were positive for abnormal prion protein, indicating an overall prevalence of 493 per million population, or one in 2,000 people are likely to be carriers. No difference was seen in different birth cohorts (1941-60 and 1961-85), in both genders, and there was no apparent difference in abnormal prion prevalence in three broad geographical areas. Genetic testing of the 16 positive samples revealed a higher proportion of valine homozygous (VV) genotype on the codon 129 of the gene encoding the prion protein (PRNP) compared with the general UK population. This also differs from the 177 patients with vCJD, all of whom to date have been methionine homozygous (MM) genotype. The concern is that individuals with this VV genotype may be susceptible to developing the condition over longer incubation periods.


In 1988, there was a confirmed death from CJD of a person from Manchester, New Hampshire in the United States. Massachusetts General Hospital believed the patient acquired the disease from a surgical instrument at a podiatrist’s office. In September 2013, another patient in Manchester, New Hampshire was posthumously determined to have died of the disease. The patient had undergone brain surgery at Catholic Medical Center three months before his death, and a surgical probe used in the procedure was subsequently reused in other operations. Public health officials identified thirteen patients at three hospitals who may have been exposed to the disease through the contaminated probe, but said the risk of anyone’s contracting CJD is “extremely low.“ In January 2015, the former speaker of the Utah House of Representatives, Rebecca D. Lockhart, died of the disease within a few weeks of diagnosis. John Carroll, former editor of The Baltimore Sun and Los Angeles Times, died of CJD in Kentucky in June 2015, after having been diagnosed in January. American actress Barbara Tarbuck (General Hospital, American Horror Story) died of the disease on December 26, 2016.


An experimental treatment was given to a Northern Irish teenager, Jonathan Simms, beginning in January 2003. The medication, called pentosan polysulphate (PPS) and used to treat interstitial cystitis, is infused into the patient’s lateral ventricle within the brain. PPS does not seem to stop the disease from progressing, and both brain function and tissue continue to be lost. However, the treatment is alleged to slow the progression of the otherwise untreatable disease, and may have contributed to the longer than expected survival of the seven patients studied. Simms died in 2011. The CJD Therapy Advisory Group to the UK Health Departments advises that data are not sufficient to support claims that pentosan polysulphate is an effective treatment and suggests that further research in animal models is appropriate. A 2007 review of the treatment of 26 patients with PPS finds no proof of efficacy because of the lack of accepted objective criteria. Scientists have investigated using RNA interference to slow the progression of scrapie in mice. The RNA blocks production of the protein that the CJD process transforms into prions. This research is unlikely to lead to a human therapy for many years. Both amphotericin B and doxorubicin have been investigated as potentially effective against CJD, but as yet there is no strong evidence that either drug is effective in stopping the disease. Further study has been taken with other medical drugs, but none are effective. However, anticonvulsants and anxiolytic agents, such as valproate or a benzodiazepine, may be administered to relieve associated symptoms.


Scientists from the University of California, San Francisco are currently running a treatment trial for sporadic CJD using quinacrine, a medicine originally created for malaria. Pilot studies showed quinacrine permanently cleared abnormal prion proteins from cell cultures, but results have not yet been published on their clinical study. The efficacy of quinacrine was also assessed in a rigorous clinical trial in the UK and the results were published in Lancet Neurology, and concluded that quinacrine had no measurable effect on the clinical course of CJD. In a 2013 paper published in the Proceedings of the National Academy of Sciences, scientists from The Scripps Research Institute reported that Astemizole, a medication approved for human use, has been found to have anti-prion activity and may lead to a treatment for Creutzfeldt-Jakob disease.


Study of WWII Evacuees Suggests Mental Illness May Be Passed to Offspring


From 1941 to 1945, roughly 49,000 Finish children were evacuated from their homes to protect them from bombings, malnutrition and other hazards during the country’s wars with the Soviet Union. The children, many of them only preschoolers, were placed with foster families in Sweden. In addition to separation from their families, the children faced the stresses of adapting to their foster families, and in many cases, learning a new language. Upon their return, many children experienced the additional stress of readjusting to Finnish society. During the same time, thousands of Finnish families chose not to evacuate all their children and often kept some at home, but little information exists on the rationale for their decisions.


According to an article published in JAMA Psychiatry (29 November 2017), a study of the adults whose parents evacuated Finland as children during World War II, suggests that mental illness associated with early childhood adversity may be passed from generation to generation,. The study was conducted by researchers at the National Institutes of Health, Uppsala University in Sweden, and Helsinki University in Finland. Results showed that daughters of female evacuees had the same high risk for mental health disorders as their mothers, even though they did not experience the same adversity. However, the study could not determine why the higher risk for mental illness persisted across generations. Possible explanations include changes in the evacuees’ parenting behavior stemming from their childhood experience or epigenetic changes — chemical alterations in gene expression, without any changes to underlying DNA.


For the study, the authors compared the risk of being hospitalized for a psychiatric (mental health) disorder among offspring of the evacuees to the risks of psychiatric hospitalization among the offspring of the siblings who remained with their parents. Studying the two groups — cousins to each other — allowed the authors to compensate for family-based factors that can contribute to mental health problems and to focus instead on the evacuees’ wartime experience.


In a previous study, the authors found that women evacuated as children were more than twice as likely to be hospitalized for a psychiatric disorder than their female siblings who remained at home. For the current study, the authors linked records from this generation — more than 46,000 siblings born between 1933 and 1944 — to those of their offspring, more than 93,000 individuals born after 1950. Of these, nearly 3,000 were offspring of parents who had been evacuated to Sweden as children, and more than 90,000 were offspring of parents who remained in Finland during the war. The authors found that female evacuees and their daughters were at the greatest risk for being hospitalized for mood disorders, such as depression and bipolar disorder. In fact, the evacuees’ daughters had more than four times the risk of hospitalization for a mood disorder, compared to the daughters of mothers who stayed home — regardless of whether their mothers were hospitalized for a mood disorder. The authors did not find any increase in psychiatric hospitalizations for the sons or daughters of males who had been evacuated as children. The study could not determine why the daughters of female evacuees had a higher risk of mental illness. One possibility is that the stresses of the evacuees’ experience affected their psychological development in ways that influenced their parenting style. Another possibility is that the evacuee experience resulted in epigenetic changes. For example, the authors cited an earlier finding that Holocaust survivors have higher levels of compounds known as methyl groups bound to the gene FKBP5 and have passed this change on to their children. This higher level of methyl groups appears to alter the production of cortisol, a hormone that regulates the stress response.


The authors concluded that future studies are needed to understand how the experience of war affects the mental health of parents and their offspring and to develop interventions to help families affected by armed conflict.


Hibernating Ground Squirrels Provide Clues to New Stroke Treatments


An ischemic stroke occurs when a clot cuts off blood flow to part of the brain, depriving those cells of oxygen and nutrients like the blood sugar glucose that they need to survive. Nearly 800,000 Americans experience a stroke every year and 87% of those are ischemic strokes. Currently, the only way to minimize stroke-induced cell death is to remove the clot as soon as possible. A treatment to help brain cells survive a stroke-induced lack of oxygen and glucose could dramatically improve patient outcomes, but no such neuroprotective agents for stroke patients exist.


In the fight against brain damage caused by stroke, the authors turned to an unlikely source of inspiration: hibernating ground squirrels. While the animals’ brains experience dramatically reduced blood flow during hibernation, just like human patients after a certain type of stroke, the squirrels emerge from their extended naps suffering no ill effects. Excitingly, a potential drug has been identified that could grant the same resilience to the brains of ischemic stroke patients by mimicking the cellular changes that protect the brains of those animals. The study was published online on 16 November  2017, in The FASEB Journal, the official journal of the Foundation of American Societies for Experimental Biology.


Recently, the authors of the study, found that a cellular process called SUMOylation goes into overdrive in a certain species of ground squirrel during hibernation. Dr. authors suspected this was how the animals’ brains survived the reduced blood flow caused by hibernation, and subsequent experiments in cells and mice confirmed his suspicions. SUMOylation occurs when an enzyme attaches a molecular tag called a Small Ubiquitin-like Modifier (SUMO) to a protein, altering its activity and location in the cell. Other enzymes called SUMO-specific proteases (SENPs) can then detach those tags, thereby decreasing SUMOylation. In the current study, the authors examined whether any of over 4,000 molecules from the NCATS small molecule collections could boost SUMOylation by blocking a SENP called SENP2, which would theoretically protect cells from a shortage of life-sustaining substances. The authors first used an automated process to examine whether the compounds prevented SENP2 from severing the connection between a tiny metal bead and an artificial SUMO protein. This system, along with computer modeling and further tests performed both in and outside of cells, whittled the thousands of candidate molecules down to eight that could bind to SENP2 in cells and were non-toxic. Two of those – ebselen and 6-thioguanine – were then found to both boost SUMOylation in rat cells and keep them alive in the absence of oxygen and glucose. A final experiment showed that ebselen boosted SUMOylation in the brains of healthy mice more than a control injection. 6-thioguanine was not tested because it is a chemotherapy drug with side effects that make it unsuitable as a potential stroke treatment. The authors now plan to test whether ebselen can protect the brains of animal models of stroke.


Puerto Rico Related Medical Product Shortages


According to FDA, while Puerto Rico is making progress in its effort to recover from the devastation left by the hurricanes, it remains a long process and there’s a lot of work left to do. At the FDA, is remaining vigilant about helping address the challenges that remain. Power is being restored across the island and, importantly, some major medical product manufacturing facilities are coming back online and stabilizing their production. However, until the grid is reliably restored, many firms will continue to run on generator power or require generators as a backup and production levels will not return to their baseline levels.


Over the last few weeks, FDA has been addressing the IV saline products shortage, which was exacerbated by Hurricane Maria. FDA has been closely working with one supplier, Baxter, to help them restore production operations in their Puerto Rico facilities. FDA also approved IV solution products from Fresenius Kabi and Laboratorios Grifols to mitigate the shortage, and both of those companies have been working to increase production of saline products. Thanks to steps like these, FDA now believes that the shortage situation related to IV saline products will improve by the end of 2017. While FDA has made progress on this front, unfortunately there continue to be drug shortage issues that are of serious concern to the agency. In addition to FDA’s ongoing concerns related to IV saline products, FDA is also are particularly focused on the shortage of amino acids for injection. This product is of critical need for patients, including children and infants, who are not able to eat and need to receive their nutrition intravenously. Like with saline, an ongoing amino acid short supply situation was worsened by Hurricane Maria’s impact on Puerto Rican drug manufacturing facilities that manufacture this product.


Most notably, the hurricane disrupted Baxter’s amino acids production facilities in Puerto Rico; Baxter is one of the largest manufacturers of this product serving the U.S. market. In order to help mitigate this shortage, the FDA has worked with Baxter to facilitate the temporary importation of amino acids for pediatric and adult formulations of IV amino acids from Baxter facilities in the United Kingdom and Italy. FDA is also working with other manufacturers of amino acids to increase supplies to address the shortage, including ICU Medical and B. Braun. ICU Medical had experienced manufacturing delays, but now plans to return to the market soon, which will further help address the shortage. FDA continues to work closely with federal and Puerto Rican authorities to address the needs of manufacturers on the island for power and other resources. These efforts have been focused on the needs of patients — to prevent potential shortages of medically important products where possible, and help ensure that any shortages that do occur are mitigated as quickly as possible. FDA does understand the burden and stress drug shortages have on patients, health care providers and hospitals. FDA is monitoring approximately 90 medical products manufactured on Puerto Rico (which includes biologics, devices and drugs) that are important to patients. Mitigating medical product shortages will require a sustained effort by industry, the agency and other partners as we work with manufacturers to return to production levels that adequately meet the needs of patients.


Turkey Biscuits Presented in Various Ways

Warm Turkey Biscuit served over a delicious parsnip puree, topped with hot gravy and sprinkled with white sesame seeds. ©Joyce Hays, Target Health Inc.


Before I share a new recipe, it goes through many iterations; however, this was delicious the first time I experimented with the ingredients. This recipe is quick and easy, which is just what you want, after all your effort to make Thanksgiving work well. ©Joyce Hays, Target Health Inc.


Turkey Biscuits served over a medley of rice, mushrooms and green peas, hot gravy and sprinkled with black sesame seeds. ©Joyce Hays, Target Health Inc.


Same dish as above, after half the turkey biscuit has been eaten, revealing a soft moist center. ©Joyce Hays, Target Health Inc.


Plain hot Turkey Biscuits on their way to the table. MMmmm, they smell so-o good. Can’t want to sink our teeth into one of these. Served with roasted asparagus, a crunchy garden salad and chilled white wine. Btw, these yummy biscuits make a great finger food. I know this, because Jules keeps grabbing them out of the fridge to snack on. ©Joyce Hays, Target Health Inc.



2 or 3 cups left-over turkey

1 pinch sea salt

1 pinch black pepper

1 teaspoon curry

1 jalapeno, seeds removed, then very well chopped

2 Tablespoons Kraft mayonnaise

2 teaspoons left-over gravy from bottom of turkey roast pan

6 fresh garlic cloves, sliced

One 2 inch piece of ginger, peeled then grated

6 scallions, thinly sliced (use the white part only)

Juice of 1/2 fresh lime

1 Tablespoon chickpea flour

1/2 teaspoon baking soda

1/2 teaspoon baking powder

1 egg, plus 1 egg white, slightly beaten in a small cup

Extra virgin olive oil for cooking

Use left-over gravy or make a new batch.


You need a food processor for this recipe and a large skillet.

Turkey Biscuits are the perfect meal for left-over roast turkey or chicken. Plus, they don’t have the same flavor as your turkey dinner. This is a quick, easy and delicious recipe; really hope you’ll try it. ©Joyce Hays, Target Health Inc.



1. Get all your slicing, egg-separating, chopping, grating, done first.


Preparing the lime and jalapeno. ©Joyce Hays, Target Health Inc.


Grating the ginger. ©Joyce Hays, Target Health Inc.


2. Get out your food processor, and a large skillet

3. All the ingredients are going to end up in your food processor, so it hardly matters, which goes in first, except, do this: add all of the dry ingredients last.


Adding wet ingredients to food processor (garlic, onion, lime, jalapeno, scallions). ©Joyce Hays, Target Health Inc.


Egg, all seasonings, gravy, turkey, mayo; all wet ingredients are now in food processor, ready to be pulsed. ©Joyce Hays, Target Health Inc.


4. Add the dry ingredients to the food processor, last. Then, pulse until all ingredients have been completely and thoroughly combined. It’s important to do this right.


After pulsing all wet ingredients, the dry ingredients were added, then pulsed. I’m going to pulse it just a little bit longer before removing from food processor. ©Joyce Hays, Target Health Inc.


5. Next, with a narrow spatula, scrape all the contents from your food processor, into a medium bowl. Get it all out, so it all goes into the Turkey Biscuits.


Batter is now ready to be hand molded into Turkey Biscuits for cooking. ©Joyce Hays, Target Health Inc.


6. Put oil in your large skillet and plan to cook no more than 3 or 4 Turkey Biscuits at a time. Use a medium high flame and heat before cooking.

7. Rub some flour together, on your hands, then with a Tablespoon, scoop out of the bowl, some of the mixture, and with your other hand, form an oval shape while mixture is still in the Tablespoon, and plop it into the hot skillet, using fingers to get all of the mixture out of the Tablespoon. There is no need to have each Turkey Biscuit look exactly the same.

8. Cook 1 to 2 minutes on each side. After flipping over the first time, you may see that this side needs to be cooked a little longer. Simply wait until the other side has cooked and browned, then flip back and cook a little longer, if needed. Both sides should be a golden brown; but not overcooked, or will be ruined.


First Turkey Biscuit to go into pan. Have some paper towel next to pan to drain the biscuits when cooked. ©Joyce Hays, Target Health Inc.


Here’s that first Turkey Biscuit after being flipped. This is just the right color to aim for, a lovely golden brown. ©Joyce Hays, Target Health Inc.


9. Have a serving platter ready, so that when cooked, you can arrange the Turkey Biscuits and serve immediately with hot gravy and a few sesame seeds (black or white) sprinkled over the Biscuits.


Turkey Biscuit cut in half, showing the yummy moist texture. Served with lots of hot gravy. ©Joyce Hays, Target Health Inc.


Turkey Biscuits are good as a quick snack; above served plain with green beans and almonds. ©Joyce Hays, Target Health Inc.


Turkey Biscuits served with cranberry sauce and gravy, over sauteed mushrooms and sweet peas. ©Joyce Hays, Target Health Inc.


We had several white wines during our testing of my new recipe for Turkey Biscuits. You can’t go wrong with some of our old standbys like the Stag’s Leap Wine Cellars, above or a Pino Grigio or another favorite, Pouilly-Fuisse, not to mention Prosecco, a Rose, Blanc de Blancs or Champagne and plenty more. ©Joyce Hays, Target Health Inc.


We went to Lincoln Center this weekend to hear Verdi’s Requium, a magnificent choral piece conducted by James Levine, whose health is better now, hence the maestro is back in the pit. Very enjoyable time!


Have a great week everyone!


From Our Table to Yours

Bon Appetit!