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Publication Abstract from PubMed

Klebsiella pneumoniae is a Gram-negative opportunistic pathogen responsible for a wide range of community-associated and hospital-acquired infections and a major cause of neonatal sepsis in low- and middle-income countries. The pathogen's surface fimbriae, particularly the Type 3 fimbriae, are critical for bacterial adhesion, biofilm formation, and host defense evasion. MrkA, the pathogen's major Type 3 fimbrial subunit, has a structural function in fimbrial assembly, but its three-dimensional structure remains to be fully elucidated. In this study, we utilized solution-state nuclear magnetic resonance spectroscopy to elucidate the structure of MrkA, leveraging previously reported chemical shift assignments of a designed self-complementing monomeric protein. Additionally, we confirmed the ability of monoclonal antibodies, capable of recognizing MrkA oligomers on wild-type Klebsiella bacteria, to bind the recombinant MrkA protein. Our findings contribute to the evaluation of MrkA as a potential target in vaccine development against Klebsiella pneumoniae infections.

Biological and structural characterization of the Type 3 fimbrial subunit MrkA from Klebsiella pneumoniae.,Monaci V, Oldrini D, Gasperini G, Banci L, Cantini F, Micoli F Protein Sci. 2025 Nov;34(11):e70343. doi: 10.1002/pro.70343. PMID:41118248^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.