Encountering Lectins In The Recipient Mucosa: Implications Of N-linked Glycosylation On HIV-1 Transmission

Although several studies have determined key differences in envelope motifs between TF and chronic HIV-1, it is still not known what the overall glycosylation profile is that is selected for in a transmission event, as well as what contributes to this selection. Using a bottom-up approach of modifying specific viruses, determining their transmission fitness in an ex vivo tissue explant assay, and determining their glycan content, we have laid the basis for determining the overall glycan structure which is selected for in TF HIV-1. Preliminarily, we have shown that C-type lectins represent a stringent barrier to transmission and have several modified viruses to be tested to determine a glycan profile that is most similar to TF HIV-1. Knowledge of the overall glycan motifs which are selected for in a transmission event provides the means necessary to target TF in a prophylactic therapy.