In response to the tremendous genetic Silmitasertib diversity of HIV, a series of monoclonal Ab capable of broadly neutralizing diverse strains of HIV across different clades have been recently discovered that not only neutralize a much greater diversity of HIV strains than previously, but also extend the in vitro geometric mean IC50 into ng/mL potencies. Because of the high affinity of typical Ab-antigen binding, it is generally assumed that these potent bnAb rapidly bind to and neutralize HIV. Our mathematical model describes the dynamics of male-tofemale HIV transmission, beginning the instant semen is ejaculated into the vaginal lumen and tracking HIV virions until they reach the vaginal epithelium. Once virions reach the epithelial lumen, virions must still access target cells in the epithelium, and intact stratified vaginal epithelia has long been believed to serve as a mechanical barrier excluding virus access. Nevertheless, HIV virions have been observed to quickly penetrate the superficial layers of the stratified epithelium in human cervical explants and the female rhesus macaque genital tract, thereby gaining access to superficial Langerhans cells and CD4 T cells. The timescale required for successful cellular penetration of HIV may be further reduced by any pre-existing micro or macro lesions in the epithelium as well as abrasions upon coital stirring. Thus, in the absence of an established mathematical model that can accurately recapitulate HIV penetration of the squamous epithelium, we chose virion passage through the CVM layer as the time scale to evaluate Ab coverage on virions. Similar assumptions were previously made by the Katz group to model the efficacy of microbicides against HIV. The vaginal epithelium is highly folded into collapsed “rugae” coated with a layer of viscoelastic and adhesive cervicovaginal mucus gel. During coitus, the epithelium becomes stretched and exposed. We thus model the vaginal epithelial surface as the inner surface of a simple cylinder coated with a roughly d=50 mm thick CVM layer containing different concentrations of elicited or topically dosed bnAb. It is important to note that there are substantial variations in the approaches used to measure binding affinities, which range from the use of monomeric gp120 binding to immobilized IgG, to Fab binding to directly immobilized monovalent gp120, to IgG binding to directly immobilized, uncleaved trimers but fitted with a model for monovalent interaction, and finally the binding of uncleaved trimers to captured Fabs, fitted with a monovalent model. The outer membrane of Gram-negative bacteria is an asymmetric membrane containing phospholipids and a unique glycolipid lipopolysaccharide in the inner and outer leaflet, respectively. OM proteins and lipoproteins are also embedded and anchored, respectively, in the OM. LPS is a complex molecule that can be structurally divided in three elements: lipid A, the hydrophobic moiety that anchors LPS in the outer membrane, the core oligosaccharide and the O-antigen. The OM mainly serves as a protective barrier enabling Gram-negative bacteria to survive in harsh environments and to exclude several toxic molecules effective against Gram-positive organisms.