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We analyzed whether the common respiratory pathogens Streptococcus pneumoniae, Haemophilus influenzae, Moraxella catarrhalis, and other bacterial species interact with antichymotrypsin. M. catarrhalis was the only species that bound antichymotrypsin among 25 bacterial species tested by flow cytometry and direct binding assay. We compared a series of clinical isolates in addition to wild-type and ubiquitous surface protein\u2013deficient Moraxella to study the nature of antichymotrypsin binding by the bacteria. Experiments with Moraxella mutants revealed that ubiquitous surface proteins A1 and A2 were responsible for the interaction, and using recombinant fragments, a consensus sequence within ubiquitous surface proteins A1 and A2 was defined. Binding of iodine-labeled antichymotrypsin was dose dependent and strong (dissociation constant [Kd] 24.9\u201344.8 nM). Moreover, a chymotrypsin activity assay showed that antichymotrypsin, when bound to the bacterial surface, was neutralized. Moraxella antichymotrypsin neutralization is a novel microbial virulence mechanism that may induce excessive inflammation resulting in more exposed extracellular matrix that is beneficial for bacterial colonization.<\/jats:p>","DOI":"10.1165\/rcmb.2007-0289oc","type":"journal-article","created":{"date-parts":[[2007,12,20]],"date-time":"2007-12-20T21:11:39Z","timestamp":1198185099000},"page":"609-617","source":"Crossref","is-referenced-by-count":11,"title":["<i>Moraxella<\/i>\n                    -Dependent \u03b11-Antichymotrypsin Neutralization"],"prefix":"10.1093","volume":"38","author":[{"given":"Taras","family":"Manolov","sequence":"first","affiliation":[{"name":"Medical Microbiology, Department of Laboratory Medicine, Malm\u00f6 University Hospital, Lund University, Malm\u00f6, Sweden; and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thuan Tong","family":"Tan","sequence":"additional","affiliation":[{"name":"Medical Microbiology, Department of Laboratory 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