Analysis of N-Glycosylation Sites in HIV glycoprotein 160

Abstract

AbstractHIV infection is a condition caused by the human immunodeficiency virus. The condition gradually destroys the immune system, which makes it harder for the body to fight infections. HIV presents a complex knot for scientists to unravel. An envelope protein of the human HIV that is encoded by the env gene contains numerous glycosylation sites. It serves as a precursor for both the GP120 and the GP41. Here statistical investigation was done to study the sequential aspects of amino acids around the N-glycosylated protein from HIV virus. Sequences containing N-glycosylated asparagine were selected from the uniprot database of N-glycosylated proteins. The frequency of occurrence of amino acid residues around the glycosylated asparagine showed that there are increased numbers of isoleucine and threonine residues around the N-glycosylation sites in comparison with the nonglycosylated asparagine residues. Preferential occurrence of amino acid residues around the glycosylation site shows that T has the maximum preference around the N-glycosylation site. T at 3 and/or -3 positions strongly favors glycosylation irrespective of other glycosylation sites. The data presented in the present work clearly indicate that there is a pronounced positional preference for the hydrophobic and neutral amino acids at various positions around the N-glycosylation site. In the future it will be of much interest to investigate further the possible structural and conformational implications of some of these suggested positional preferences of the various amino acids around the site of glycosylation. This is a potentially important study, and such analyses will surely contribute an important part of our knowledge base in the future on HIV research. These results will be of interest to molecular biologists and protein engineers to identify N-glycosylation sites important in molecular recognition processes in HIV virus.