ArticleBiochemical and biophysical research communications2018
The HMW2 adhesin of non-typeable Haemophilus influenzae is a human-adapted lectin that mediates high-affinity binding to 2-6 linked N-acetylneuraminic acid glycans.
Article in Biochemical and biophysical research communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Adaptation of NontypeablemBio · 2023Article
- The alginate polymer OligoG alters susceptibility of biofilm-embedded non-typeableJAC-antimicrobial resistance · 2023Article
- Non-typeableFrontiers in cellular and infection microbiology · 2023Article
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- Article
- Nontypeable Haemophilus influenzae Type IV Pilus Mediates Augmented Adherence to Rhinovirus-Infected Human Airway Epithelial Cells.Infection and immunity · 2020Article
- Panel 7 - Pathogenesis of otitis media - a review of the literature between 2015 and 2019.International journal of pediatric otorhinolaryngology · 2020Review
- NontypeablemBio · 2019Article
- Natural and Synthetic Sialylated Glycan Microarrays and Their Applications.Frontiers in molecular biosciences · 2019Review
- Article
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7 authors.
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Abstract
Non-typeable Haemophilus influenzae (NTHi) is a human-adapted bacterial pathogen, responsible for infections of the human respiratory tract. This pathogen expresses a range of adhesins that mediate binding to host cells. Most NTHi strains can express the related adhesins HMW1 and HMW2. Expression of HMW proteins is phase-variable: changes in the length of simple-sequence repeats located in the encoding genes promoter regions results in changes in expression levels of these adhesins. HMW expression is also controlled by epigenetic regulation. HMW1 has been previously demonstrated to bind α 2-3 sialyl-lactosamine, but affinity of this interaction has not been investigated. The host receptor(s) for HMW2 is currently unknown. We hypothesized that host glycans may act as receptors for HMW2-mediated adherence. We examined the glycan-binding activity of HMW2 using glycan arrays and Surface Plasmon Resonance (SPR). These studies demonstrate that HMW2 binds 2-6 linked N-acetylneuraminic acid with high affinity. HMW2 did not bind glycan structures containing the non-human form of sialic acid, N-glycolylneuraminic acid. Thus, the specificity of HMW1 and HMW2 have complementary lectin activities that may allow NTHi distinct niches in the human host.
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