This update was originally written by BioClonetics CEO/President Charles Cotropia

BioClonetics is validating its anti-HIV monoclonal antibody technology having now produced quantity and quality sufficient recombinant antibodies for neutralization studies. 

As background, the parent Clone 3 monoclonal antibody demonstrated effectiveness by neutralizing 95% (41/43) of HIV isolates against which it was tested in 5 international labs.  In these tests, the parent antibody was tested in the more stringent PMBC-based in vitroneutralization assay test methodology. In such tests, an antibody is tested against live HIV viruses. 

We have now produced recombinants of the parent antibody, a form required by the FDA for use in clinical trials and patient therapy. These recombinants have demonstrated much stronger binding to HIV gp41, indicating that their neutralization capability is expected to be more potent than the parent antibody.

Testing of the recombinants in the PBMC-based neutralization assay tests is significant in that it is far more reliable than other “rapid tests” methodologies (such as the TZM.bl assay test) that have been designed to provide quick results but results that do not have concordance with the more direct and sophisticated PBMC-based neutralization assay tests.

We have engaged two labs with the expertise and capability to conduct the more sophisticated PBMC-based neutralization tests on our recombinant antibodies.

·       Texas Biomedical Research Institute, San Antonio, Texas, currently has our recombinant antibodies for testing.

·       Retrovirox has been engaged to test our recombinant antibodies against 10 different HIV isolates - completion of testing is expected in August 2018.

Based on the significant binding studies of the recombinant against gp41 on the HIV virus, we expect favorable results from such tests. Thereafter, the antibodies will be tested in macaques at the Southwest National Primate Research Center, in San Antonio, Texas. These tests will provide validation of efficacy of our antibody and the expected successful results in clinical trials and patient therapy.

A Second Therapy is Also Now Being Created

From our technology, we have also just initiated a separate and highly complementary therapeutic approach to treating HIV.

As described, from the parent antibody, a first recombinant antibody form (called the IgG antibody structure) has been created. And noted, these recombinants are scheduled to be tested in PBMC-based assays against HIV isolates in two separate labs.

This IgG antibody form of our antibody protects against HIV replication within the human blood circulatory system. In other words, this form of the antibody (the IgG antibody structure) prevents the virus from replicating in the human body – a step critical to providing an HIV cure.

But, there is another functional antibody category called "IgA antibody” that can be used against HIV. IgA antibodies protect against HIV infections that occur at mucosal surfaces, specifically, for example, vaginal, anal and oral mucosal surfaces of the human body. HIV exposure at the mucosal surfaces accounts for the majority of HIV infections which occur upon initial contact with the HIV virus.

We have this week initiated the creation of this IgA structure from our existing IgG structure using a process called "class switching". This process uses currently available biotechnological methodology – starting with our now known recombinant IgG antibody structure and producing the IgA structure – resulting in an additional protective structural class of antibodies. This therapy will expectedly provide a protective immunological defense against initial exposure to HIV virus at mucosal surfaces, such as occurs in the passage of the virus from mother to child through maternal breastfeeding.

We are now producing this second line of defense.  Preparation of this IgA structure is in progress as this update is being prepared.