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EP-4125858-B1 - NUTRITIONAL COMPOSITION COMPRISING L-CARNITINE TARTRATE FOR USE IN TREATING OR PREVENTING A CORONAVIRUS INFECTION IN A MAMMAL

EP4125858B1EP 4125858 B1EP4125858 B1EP 4125858B1EP-4125858-B1

Inventors

  • BELLAMINE, Aoutef
  • DURKEE, SHANE

Dates

Publication Date
20260506
Application Date
20210119

Claims (6)

  1. An angiotensin-converting enzyme 2 (ACE-2) reducing nutritional supplement comprising an ACE-2 reducing component for the use in the treatment, prevention, and/or delay of progression of infection in a mammal caused by an infectious agent which binds to the (ACE-2) in the mammal, wherein the infectious agent comprises a corona virus, wherein the ACE-2 reducing component is L-carnitine tartrate, and wherein said nutritional supplement comprises a) L-carnitine tartrate; and b) an auxiliary substance.
  2. The nutritional supplement for use according to claim 1, wherein the ACE-2 reducing component is administered orally, nasally, intravenously, intramuscularly or transdermally to the mammal.
  3. The nutritional supplement for use according to claim 1 or 2, further comprising administering the ACE-2 reducing component to the mammal, prior to the onset of an infection or during the infection from the infectious agent.
  4. The nutritional supplement for use according to any one of claims 1-3, wherein the carnitine is administered to the mammal once or twice a day, and wherein the ACE-2 reducing component ACE-2 component is administered in an amount between about 5mg and 10,000 mg per day, typically between about 250 mg and 5000 mg per day, more typically between about 500 and 4000 mg per day.
  5. The nutritional supplement for use according to any one of the preceding claims 1-4, wherein the corona virus is SARS-COV-2.
  6. The nutritional supplement for use according to any one of claims 1-5, wherein the an auxiliary substance comprises at least one of excipients, binders, carriers, antiseptics, antioxidants, disintegrators, lubricants, flavoring agents, or a combination of two or more.

Description

The present application claims priority to U.S. Provisional Application Serial No. 63/016,579, filed on April 28, 2020, U.S. Provisional Application Serial No. 63/028,934, filed on May 22, 2020, and U.S. Provisional Application Serial No. 63/112,942 filed on November 12, 2020. BACKGROUND L-carnitine was first discovered in 1905. Since then, extensive research has demonstrated the important role it plays in helping bodies utilize dietary fat for energy. Without sufficient L-carnitine in the body, humans and animals would not be able to utilize fat effectively and long-term health problems may occur. In the body, L-carnitine is known to shuttle long-chain fatty acids across the inner-mitochondrial membrane so that the fatty acids can be metabolized and converted into energy. Without L-carnitine, these fatty acids would not be transported and properly utilized. Mammals can obtain L-carnitine naturally from two sources. First, L-carnitine can be biosynthesized within the body. The body, however, can only produce small amounts of L-carnitine. L-carnitine can also be obtained from foods, such as red meat. The assignee of the present disclosure markets a L-carnitine and salts thereof as nutritional supplements for mammal application. In the past, L-carnitine and derivatives and salts thereof have been administered to mammals. For instance, L-carnitine and derivatives and/or salts thereof can be administered to a mammal when the diet of the mammal is low in L-carnitine. L-carnitine and derivatives and salts thereof have also been administered to mammals in order to prevent obesity, for heart health and other various health reasons. L-carnitine and derivatives and salts thereof have also been marketed to older or senior pets. As mammals increase in age, for instance, the availability of L-carnitine in the body decreases because food intake normally decreases and the body's ability to produce L-carnitine begins to drop. Supplementation with L-carnitine and derivatives and/or salts thereof has shown a positive influence on the aging process. Severe acute respiratory syndrome coronavirus (SARS-CoV-1 and SARS-CoV-2) has been responsible for the SARS epidemic in 2002 to 2004 and more recently for the coronavirus disease 2019 (Covid-19) pandemic outbreak initially detected in December 2019. The disease is caused by the SARS-CoV-2, an airborne virus that affects mainly the lungs and the upper respiratory system, leading ultimately to lung injury, respiratory distress and death in severe cases. Coronaviruses (CoVs) are enveloped positive-sense RNA viruses, and are characterized by club-like spikes that project from their surface, an unusually large RNA genome, and a unique replication strategy. These spike projection contains protein domains responsible for its interaction with host cells and its entry in these cells. Coronaviruses cause a variety of diseases in mammals and birds ranging from enteritis in cows and pigs and upper respiratory disease chickens to potentially lethal human respiratory infections. The presence of a novel coronavirus pandemic in 2019 (COVID-19) has posed threat to the world population of humans. A recent study has confirmed that severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uses a severe acute respiratory syndrome coronavirus (SARS-CoV) receptor, the angiotensin-converting enzyme 2 (ACE-2) of the host cell, to attach to the host mammal. See Hoffmann M, Kleine-Weber H, Schroeder S, Kruger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, et al. SARS-CoV-2 Cell Entry Depends On ACE-2 And TMPRSS2 And Is Blocked By A Clinically Proven Protease Inhibitor. Cell. 2020; 181:1-10. ACE-2 expression was previously found to correlate with increase susceptibility to SARS-CoV infection in vitro. Hofmann H, Geier M, Marzi A, Krumbiegel M, Peipp M, Fey GH, Gramberg T, Pohlmann S., Susceptibility To SARS Coronavirus S Protein-Driven Infection Correlates With Expression Of Angiotensin Converting Enzyme 2 And Infection Can Be Blocked By Soluble Receptor. Biochem Biophys Res Commun. 2004; 319:1216-1221. As with SARS-CoV-2, higher ACE-2 expression might also lead to higher risk of COVID-19 infection. Following its binding to the ACE-2 receptor, the SARS-CoV-2 spike protein is further cleaved to facilitate its entry to the host cell. Cleavage is believed to be mediated by TMPRSS2 (transmembrane protease serine 2) at the position S1/S2 and Furin at the S' position. Further, a Furin-like cleavage site has been discovered in the spike protein of the SARS-CoV-2, that is not present in other SARS-like CoVs. It is believed that Furin also plays a part in the a Coronavirus 2019 infection. B. Coutarda, et al., The Spike Glycoprotein of the New Coronavirus 2019-nCoV Contains a Furin-like Cleavage Site Absent in CoV of the Same Clade, Antiviral Research 176 (2020) 104742. Other coronaviruses, such as the Middle East Respiratory Syndrome-CoV (MERS-CoV) utilizes Dipeptidyl peptidase 4 (DPP-4) as