Document Type

Plan B - Open Access

Award Date


Degree Name

Master of Science (MS)


Biology and Microbiology

First Advisor

Greg Heiberger


The tendency for the Human Immunodeficiency Virus (HIV) to proliferate and mutate it’s trimeric envelop (Env), is one of the reasons why it’s a challenge for an antibody-based vaccine to be developed. Glycoprotein 160 (gp160,) which consists of glycoprotein 120 (gp120) and glycoprotein 41 (gp41), is the main focus for a research vaccine design. Gp120 consists of an outer membrane, inner membrane and bridging sheet. The protein is trimeric, and non-covalently binds to gp41. The outer domain is where the neutralizing antibody bind, such as 2G12, immunoglobulin G1b12, and anti-V3 antibodies. V3 stands for the Variable loop 3, gp120 has 5 variable loops that contribute to the binding of the envelope to the CD4 binding sites. These loops are important in immunogenicity and the binding of monoclonal neutralizing antibodies (mNAb). The V3 loop has a conserved structural element despite its variation sequence, and due to this conserved element, the anti-V3 antibodies can recognize and neutralize the virus. The anti-V3 antibodies can tolerate the sequence changes in the V3 loop in certain strains of the virus and at a certain stage of infection in patients, but this is still controversial. This paper will look at the challenges in developing body neutralizing antibodies, and the potency for anti-V3 mature antibody to neutralize and decrease the viral load during infection. It will also cover recent and future vaccine trials using variable loops to directly neutralize viral fusion.



Number of Pages



South Dakota State University


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