Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species.

Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species. Research Abstract Details 

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Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species. Abstract Text:

Michiko Mitsuishi,Seiko Masuda,Ichiro Kudo,Makoto Murakami,Michiko Mitsuishi,Seiko Masuda,Ichiro Kudo,Makoto Murakami,Michiko Mitsuishi,Seiko Masuda,Ichiro Kudo,Makoto Murakami,

Of 10 mammalian secreted phospholipase A(2) (sPLA(2)) enzymes identified to date, group V and X sPLA(2)s, which are two potent plasma membrane-acting sPLA(2)s, are capable of preventing host cells from being infected with adenovirus, and this anti-viral action depends on the conversion of phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) in the host cell membrane. Here, we show that human group III sPLA(2), which is structurally more similar to bee venom PLA(2) than to other mammalian sPLA(2)s, also has the capacity to inhibit adenovirus infection into host cells. Mass spectrometry (MS) demonstrated that group III sPLA(2) hydrolyzes particular molecular species of PC to generate LPC in human bronchial epithelial cells. Remarkably, in addition to the catalytically active sPLA(2) domain, the N-terminal, but not C-terminal, domain unique to this enzyme was required for the anti-adenovirus effect. To our knowledge, this is the first demonstration that the biological action of group III sPLA(2) depends on its N-terminal domain. Finally, our MS analysis provided additional and novel evidence that group III, V and X sPLA(2)s target distinct phospholipid molecular species in cellular membranes.

Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species. Publishing Authors By Initials

M Mitsuishi,S Masuda,I Kudo,M Murakami,M Mitsuishi,S Masuda,I Kudo,M Murakami,M Mitsuishi,S Masuda,I Kudo,M Murakami,

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Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biochimica et biophysica acta

VOLUME: 1771

Page Numbers: 1389-96

Journal Abbreviation: Biochim. Biophys. Acta

ISSN: 0006-3002

DAY: 10

MONTH: 10

YEAR: 2007

Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species. Information

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LANGUAGE: eng

NlmUniqueID: 217513

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Grant and Affiliation Information for Human group III phospholipase A(2) suppresses adenovirus infection into host cells Evidence that group III, V and X phospholipase A(2)s act on distinct cellular phospholipid molecular species.

AFFILIATION: Department of Health Chemistry, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.

Country: Netherlands

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MEDLINETA: Biochim Biophys Acta

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