ArticleFrontiers in cellular and infection microbiology2026
Galectin-8 binds HIV envelope glycoproteins with high affinity and promotes viral infectivity.
Article in Frontiers in cellular and infection microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- HIV-1 interactions with sialic acid-binding bacterial lectins promote virus infectivity in vitro and mucosal transmission in humanized mice.bioRxiv : the preprint server for biology · 2026Article
- HIV-1 interactions with sialic acid-binding bacterial lectins promote virus infectivityFrontiers in cellular and infection microbiology · 2026Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Target cell entry of HIV-1 is dependent on the binding of gp120, the outer component of the viral envelope glycoprotein complex (Env), to CD4 and a coreceptor, preferentially CCR5 or CXCR4. Still, other interactions may also contribute to the infectivity of the virus. One such interaction is between the highly glycosylated gp120 and carbohydrate-binding proteins, such as galectins. Here, we studied the interaction between HIV-1 Env and a panel of galectins and found that galectin-8 (Gal-8), bound with highest affinity (K
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