ArticleFrontiers in cellular and infection microbiology2026
Three hydrophobic surface binding a proteins link surface hydrophobicity to sporulation, biofilm formation, and host interaction in
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. Not yet cited in PubMed.
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Abstract
Introduction: Methods: Here, we present a comprehensive characterization of three HsbA proteins in Results: All examined HsbA proteins share a conserved α-helical fold with a hydrophobic core and are capable of binding fatty acids, while displaying differential affinity for hydrophobic interfaces. Discussion: These structural properties translate into distinct surface-associated functions, including modulation of surface hydrophobicity, biofilm formation, and sporangial architecture. Genetic analyses further demonstrate that HsbA proteins play a central role in developmental regulation, affecting spore germination timing, stress responses, sporulation, and spore hydrophobicity. At the host interaction level, HsbA overexpression increases early phagocytic uptake but impairs infection progression, whereas gene disruption enhances virulence in
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