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A domino-like chlamydial attachment process: Parachlamydia acanthamoebae attachment to amoebae is concurrently required for several amoebal released molecules and serine-protease activity

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Title: A domino-like chlamydial attachment process: Parachlamydia acanthamoebae attachment to amoebae is concurrently required for several amoebal released molecules and serine-protease activity
Authors: Hayashi, Yasuhiro Browse this author →KAKEN DB
Imin, Y. Browse this author
Matsuo, Junji Browse this author →KAKEN DB
Nakamura, Shinji Browse this author →KAKEN DB
Kunichika, Miyuki Browse this author
Yoshida, Mitsutaka Browse this author
Takahashi, Kaori Browse this author
Yamaguchi, Hiroyuki Browse this author →KAKEN DB
Issue Date: Jun-2012
Publisher: Society for General Microbiology
Journal Title: Microbiology
Volume: 158
Issue: 6
Start Page: 1607
End Page: 1614
Publisher DOI: 10.1099/mic.0.057190-0
PMID: 22403190
Abstract: Parachlamydia acanthamoebae is an obligate intracellular bacterium that infects free-living amoebae (Acanthamoeba), and is a potential human pathogen associated with hospital-acquired pneumonia. The attachment mechanism of this bacteria to host cells is a crucial step in bacterial pathogenesis, yet remains undetermined. Hence, we established monoclonal antibodies (mAbs) specific to either P. acanthamoebae or amoebae in an attempt to elucidate the involved attachment mechanism. Hybridomas of 954 clones were assessed, and we found four mAbs (mAb38, mAb300, mAb311, mAb562) that were reactive to the amoebae significantly inhibited bacterial attachment. All mAbs recognized amoebal released molecules, and mAb311 also recognized the amoebal surface. MAbs reacted with the bacteria not only in amoebae, but also those released from amoebae (except mAb311). Furthermore, serine-protease inhibitor had an inhibitory effect on the bacterial attachment to amoebae, although none of the mAbs had any synergetic effect on the attachment inhibition by the protease inhibitor. Taken together, we concluded that P. acanthoamebae attachment to amoebae is concurrently required for several amoebal released molecules and serine-protease activity, implying the existence of a complicated host-parasite relationship.
Type: article (author version)
URI: http://hdl.handle.net/2115/52906
Appears in Collections:保健科学院・保健科学研究院 (Graduate School of Health Sciences / Faculty of Health Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 山口 博之

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