Staphylococci, whether beneficial commensals or pathogens, often colonize human skin, potentially leading to competition for the same niche. In this multidisciplinary study we investigate the structure, binding specificity, and mechanism of adhesion of the Aap lectin domain required for skin colonization and compare its characteristics to the lectin domain from the orthologous adhesin SasG. The Aap structure reveals a legume lectin-like fold with atypical architecture, showing specificity for N-acetyllactosamine and sialyllactosamine. Bacterial adhesion assays using human corneocytes confirmed the biological relevance of these Aap-glycan interactions. Single-cell force spectroscopy experiments measured individual binding events between Aap and corneocytes, revealing an extraordinarily tight adhesion force of nearly 900 nN and a high density of receptors at the corneocyte surface. The SasG lectin domain shares similar structural features, glycan specificity, and corneocyte adhesion behavior. We observe cross-inhibition of Aap-and SasG-mediated staphylococcal adhesion to corneocytes. Together, these data provide insights into staphylococcal interspecies competition for skin colonization and suggest potential avenues for inhibition of colonization.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9900903PMC
http://dx.doi.org/10.1101/2023.01.26.525635DOI Listing

Publication Analysis

Top Keywords

skin colonization
12
lectin domain
12
staphylococcal interspecies
8
interspecies competition
8
competition skin
8
adhesion
5
mechanistic basis
4
basis staphylococcal
4
skin
4
colonization
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!