iScience (Aug 2024)

HIV-1 interaction with an O-glycan-specific bacterial lectin enhances virus infectivity and resistance to neutralizing antibodies

  • Daniel W. Heindel,
  • Dania M. Figueroa Acosta,
  • Marisa Goff,
  • Clauvis Kunkeng Yengo,
  • Muzafar Jan,
  • Xiaomei Liu,
  • Xiao-Hong Wang,
  • Mariya I. Petrova,
  • Mo Zhang,
  • Manish Sagar,
  • Phillip Barnette,
  • Shilpi Pandey,
  • Ann J. Hessell,
  • Kun-Wei Chan,
  • Xiang-Peng Kong,
  • Benjamin K. Chen,
  • Lara K. Mahal,
  • Barbara A. Bensing,
  • Catarina E. Hioe

Journal volume & issue
Vol. 27, no. 8
p. 110390

Abstract

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Summary: Bacteria dysbiosis and its accompanying inflammation or compromised mucosal integrity is associated with an increased risk of HIV-1 transmission. However, HIV-1 may also bind bacteria or bacterial products to impact infectivity and transmissibility. This study evaluated HIV-1 interactions with bacteria through glycan-binding lectins. The Streptococcal Siglec-like lectin SLBR-N, a part of the fimbriae shrouding the bacteria surface that recognizes α2,3 sialyated O-linked glycans, was noted for its ability to enhance HIV-1 infectivity in the context of cell-free infection and cell-to-cell transfer. Enhancing effects were recapitulated with O-glycan-binding plant lectins, signifying the importance of O-glycans. N-glycan-binding bacterial lectins FimH and Msl had no effect. SLBR-N was demonstrated to capture and transfer infectious HIV-1 virions, bind to O-glycans on HIV-1 Env, and increase HIV-1 resistance to neutralizing antibodies targeting different regions of Env. This study highlights the potential contribution of O-glycan-binding lectins from commensal bacteria at the mucosa in promoting HIV-1 infection.

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