ArticleRetrovirology2026
Functional dissection of the prototype foamy virus glycoprotein heparan sulfate binding site.
Article in Retrovirology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
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Abstract
backgroundThe foamy virus (FV) glycoprotein complex (GPC) facilitates exceptionally broad species and tissue tropism. While cell surface heparan sulfate (HS) serves as a known attachment factor, it is not essential for viral entry. Recent high-resolution structures of GPCs from various FV species identified an evolutionarily conserved, positively charged surface patch (PCSP) on the receptor-binding domain (RBD) as a putative HS-binding site (HSBS). To date, only the gorilla FV (SFVggo) HSBS has been functionally characterized, demonstrating the role of basic PCSP residues in HS-dependent attachment. Experimental evidence supporting a universal role for the GPC PCSP across other FV species is currently lacking.
resultsThe prototype FV (PFV) GPC PCSP consists of four central residues surrounded by five peripheral, positively charged residues. Using charge-switch mutagenesis, we investigated the functional role of eight PCSP residues. The central residues-K
conclusionsThe minimal HSBS of the PFV GPC is defined by four central, evolutionarily conserved positively charged residues. Substituting these with negatively charged amino acids abolishes HS-dependent attachment and severely reduces specific infectivity. The minor impact of the peripheral residue mutation K
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