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Advisor(s)
Abstract(s)
Heparan sulfate proteoglycans are known to assist HIV-1 entry into host cells, mediated by the viral envelope glycoprotein gp120. We aimed to determine the general structural features of glycosaminoglycans that enable their binding to gp120, by surface plasmon resonance. Binding was found to be dependent on sequence type, size and sulfation patterns. HIV-1 gp120 prefers heparin and heparan sulfate (with at least 16 monomers in length) over chondroitin and dermatan. Sulfate groups were essential to promote this interaction. These results advance the understanding of the molecular-level requirements for virus attachment and cell entry.
Description
© Springer-Verlag Wien 2013
Keywords
HIV-1 gp120 Viral attachment Heparan sulfate proteoglycans Glycosaminoglycans Surface plasmon resonance
Pedagogical Context
Citation
Arch Virol (2014) 159:555–560
Publisher
Springer
