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Role of OmpA1 and OmpA2 in Aggregatibacter actinomycetemcomitans and Aggregatibacter aphrophilus serum resistance
Umeå University, Faculty of Medicine, Department of Odontology.
Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Odontology.ORCID iD: 0000-0002-7948-9464
2019 (English)In: Journal of Oral Microbiology, ISSN 2000-2297, E-ISSN 2000-2297, Vol. 11, no 1, article id 1536192Article in journal (Refereed) Published
Abstract [en]

Aggregatibacter actinomycetemcomitans and Aggregatibacter aphrophilus belong to the HACEK group of fastidious Gram-negative organisms, a recognized cause of infective endocarditis. A. actinomycetemcomitans is also implicated in aggressive forms of periodontitis. We demonstrated that A. aphrophilus strains, as A. actinomycetemcomitans are ubiquitously serum resistant. Both species encode two Outer membrane protein A paralogues, here denoted OmpA1 and OmpA2. As their respective pangenomes contain several OmpA1 and OmpA2 alleles, they represent potential genotypic markers. A naturally competent strain of A. actinomycetemcomitans and A. aphrophilus, respectively were used to elucidate if OmpA1 and OmpA2 contribute to serum resistance. Whereas OmpA1 was critical for survival of A. actinomycetemcomitans D7SS in 50% normal human serum (NHS), serum resistant ompA1 mutants were fortuitously obtained, expressing enhanced levels of OmpA2. Similarly, OmpA1 rather than OmpA2 was a major contributor to serum resistance of A. aphrophilus HK83. Far-Western blot revealed that OmpA1AA, OmpA2AA, and OmpA1AP can bind to C4-binding protein, an inhibitor of classical and mannose-binding lectin (MBL) complement activation. Indeed, ompA1 mutants were susceptible to these pathways, but also to alternative complement activation. This may at least partly reflect a compromised outer membrane integrity but is also consistent with alternative mechanisms involved in OmpA-mediated serum resistance.

Place, publisher, year, edition, pages
Taylor & Francis, 2019. Vol. 11, no 1, article id 1536192
Keywords [en]
Aggregatibacter actinomycetemcomitans, Aggregatibacter aphrophilus, serum resistance, outer membrane protein A
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-153103DOI: 10.1080/20002297.2018.1536192ISI: 000448422100001Scopus ID: 2-s2.0-85055581204OAI: oai:DiVA.org:umu-153103DiVA, id: diva2:1261365
Available from: 2018-11-07 Created: 2018-11-07 Last updated: 2018-11-07Bibliographically approved

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Lindholm, MarkAung, Kyaw MinWai, Sun NyuntOscarsson, Jan

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Lindholm, MarkAung, Kyaw MinWai, Sun NyuntOscarsson, Jan
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Journal of Oral Microbiology
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