Human group III phospholipase A 2 suppresses adenovirus infection into host cells
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, ISSN: 1388-1981, Vol: 1771, Issue: 11, Page: 1389-1396
2007
- 29Citations
- 22Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations29
- Citation Indexes29
- 29
- CrossRef25
- Captures22
- Readers22
- 20
Article Description
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1388198107002090; http://dx.doi.org/10.1016/j.bbalip.2007.09.006; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=36749018033&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17980167; https://linkinghub.elsevier.com/retrieve/pii/S1388198107002090; https://dx.doi.org/10.1016/j.bbalip.2007.09.006
Elsevier BV
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