{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T05:04:26Z","timestamp":1791263066797,"version":"4.1.0"},"reference-count":60,"publisher":"Microbiology Society","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,9,1]]},"abstract":"<jats:p><jats:italic>Listeria<\/jats:italic>adhesion protein (LAP), an alcohol acetaldehyde dehydrogenase (<jats:italic>lmo1634<\/jats:italic>), interacts with host-cell receptor Hsp60 to promote bacterial adhesion during the intestinal phase of<jats:italic>Listeria monocytogenes<\/jats:italic>infection. The LAP homologue is present in pathogens (<jats:italic>L. monocytogenes<\/jats:italic>,<jats:italic>L. ivanovii<\/jats:italic>) and non-pathogens (<jats:italic>L. innocua<\/jats:italic>,<jats:italic>L. welshimeri<\/jats:italic>,<jats:italic>L. seeligeri<\/jats:italic>); however, its role in non-pathogens is unknown. Sequence analysis revealed 98\u200a% amino acid similarity in LAP from all<jats:italic>Listeria<\/jats:italic>species. The N-terminus contains acetaldehyde dehydrogenase (ALDH) and the C-terminus an alcohol dehydrogenase (ADH). Recombinant LAP from<jats:italic>L. monocytogenes<\/jats:italic>,<jats:italic>L. ivanovii<\/jats:italic>,<jats:italic>L. innocua<\/jats:italic>and<jats:italic>L. welshimeri<\/jats:italic>exhibited ALDH and ADH activities, and displayed strong binding affinity (<jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub>2\u201331\u2005nM) towards Hsp60. Flow cytometry, ELISA and immunoelectron microscopy revealed more surface-associated LAP in pathogens than non-pathogens. Pathogens exhibited significantly higher adhesion (<jats:italic>P<\/jats:italic>&lt;0.05) to Caco-2 cells than non-pathogens; however, pretreatment of bacteria with Hsp60 caused 47\u201392\u200a% reduction in adhesion only in pathogens. These data suggest that biochemical properties of LAP from pathogenic<jats:italic>Listeria<\/jats:italic>are similar to those of the protein from non-pathogens in many respects, such as substrate specificity, immunogenicity, and binding affinity to Hsp60. However, protein fractionation analysis of extracts from pathogenic and non-pathogenic<jats:italic>Listeria<\/jats:italic>species revealed that LAP was greatly reduced in intracellular and cell-surface protein fractions, and undetectable in the extracellular milieu of non-pathogens even though the<jats:italic>lap<\/jats:italic>transcript levels were similar for both. Furthermore, a LAP preparation from<jats:italic>L. monocytogenes<\/jats:italic>restored adhesion in a<jats:italic>lap<\/jats:italic>mutant (KB208) of<jats:italic>L. monocytogenes<\/jats:italic>but not in<jats:italic>L. innocua<\/jats:italic>, indicating possible lack of surface reassociation of LAP molecules in this bacterium. Taken together, these data suggest that LAP expression level, cell-surface localization, secretion and reassociation are responsible for LAP-mediated pathogenicity and possibly evolved to adapt to a parasitic life cycle in the host.<\/jats:p>","DOI":"10.1099\/mic.0.036509-0","type":"journal-article","created":{"date-parts":[[2010,5,28]],"date-time":"2010-05-28T00:46:08Z","timestamp":1275007568000},"page":"2782-2795","source":"Crossref","is-referenced-by-count":98,"title":["LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species"],"prefix":"10.1099","volume":"156","author":[{"given":"Balamurugan","family":"Jagadeesan","sequence":"first","affiliation":[{"name":"Molecular Food Microbiology Laboratory, Department of Food Science, 745 Agriculture Mall Drive, Purdue University, West Lafayette, IN 47907, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ok 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