BS, Biochemistry & Biology
California State University - San Bernadino
San Bernadino, CA
MD, PhD Student
James Munro, PhD, Rotation Adviser
HIV broadly neutralizing antibodies (bNAbs) can neutralize many viral strains of HIV. One promising bNAb targets the envelope glycoprotein 120 (gp120) that interacts with CD4 receptors of immune cells. Most antibodies generated against HIV during the first one to two years of infection are typically strain specific, however a very small percentage have been observed to be broad neutralizing. Defining the structure and characterizing the binding of the bNAb are clinically relevant studies for eliciting similar antibodies in humans. Using single molecule fluorescence energy transfer (smFRET) we should be able to investigate the proposed dynamic interactions between gp120 and potential bNAbs. My rotation project focused on fluorescent labeling a couple of mutant gp120 bNAbs with single cysteine amino acid substitutions at specific sites that would be compatible with smFRET. The dye used was maleimide coupled and I assessed the efficiency of the tag versus our wild type gp120 bNAbs.