Enzolytics Inc (ENZC)

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Why is ENZC different from other antibodies?

CEOCFO: From your recent press release, you have a proprietary methodology for producing fully human OGG1 monoclonal antibodies. How is your approach different?

There are an infinite number of distinct anti-HIV and anti-CoronaVirus monoclonal antibodies that can exist – some disease neutralizing, some perhaps of no benefit and some perhaps disease enhancing. Thus, specific antibodies that neutralize are necessary to provide an effective therapy. Enzolytics’ method of producing effective monoclonal antibodies focuses on identifying immutable binding sites on the virus and then creating monoclonal antibodies that bind to such sites and neutralize the virus. In this way, the virus cannot mutate around the therapy. For example, the antibodies administered to President Trump to treat him for the CoronaVirus, may target a site on the virus that will mutate. Thus, the same antibodies may not be effective for you or me later if the CoronaVirus has mutated, changed structure, at this binding site. Our anti-HIV monoclonal antibody binds to a site on the HIV virus that is conserved in 98% of the more than 6000 strains of the HIV-1 viruses now known, sequenced and archived in the Los Alamos National Laboratory HIV Database. The same will have to be achieved for successful anti-CoronaVirus monoclonal antibodies.

CEOCFO: From your recent press release, you have a proprietary methodology for producing fully human OGG1 monoclonal antibodies. How is your approach different?

In contrast, our method starts with human "immune-B cells", obtained from convalescent individuals who have recovered from the target virus. The primary distinction of our process for creating fully human monoclonals is the starting point – namely from human “immune-B cells” obtained from humans who have survived successfully from a "natural" infection. From these human “immune-B cells”, we then produce antibodies that target conserved immutable sites (neutralizable epitopes) on the virus’ surface envelope proteins – which will thereby avoid “virus escape”, which has been frequently demonstrated to occur as a consequence of mutations in the HIV virus surface structure.

Additionally, our antibodies retain the original natural antibody affinity and specificity, and have lower risk of immunogenicity when used as a therapeutic. They will provide broad-spectrum coverage against viral variants with increased potency, stability as a single-domain molecule, in what is called the camelid structure form, and, in the recombinant form will have greater accessibility to the virus binding sites not accessible with a whole antibody. We believe that our method is one that produces an antibody which will be more effective with less risk of adverse reaction.




Source: https://www.ceocfointerviews.com/enzolytics20.html