2002年6月
Human surfactant protein D (SP-D) binds Mycoplasma pneumoniae by high affinity interactions with lipids
JOURNAL OF BIOLOGICAL CHEMISTRY
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- 巻
- 277
- 号
- 23
- 開始ページ
- 20379
- 終了ページ
- 20385
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1074/jbc.M201089200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Increasing evidence now identifies surfactant protein D (SP-D) as an important element of the innate immune system of the lung. In this study, we examined the interactions of rat and human SP-D with the human pathogen, Mycoplasma pneumoniae. Rat and human SP-D bound the organism with high affinity in a reaction that required Ca2+ and was inhibited by EGTA. Membranes derived from the organism bound the proteins in a similar manner, except the rat SP-D also exhibited a significant level of Ca2+-independent binding. Pretreatment of membranes with proteases did not alter the Ca2+-dependent SP-D binding of membranes by either protein. Mannose, glucose, maltose, and inositol, at millimolar concentrations, competed for human SP-D binding to the bacterial membrane. Lipids extracted from membranes and separated by two-dimensional thin layer chromatography bound human SP-D with high affinity in a Ca2+-dependent reaction. A tandem mutant of SP-D with E321Q and N323D substitutions, failed to bind M. pneumoniae lipids, directly implicating the carbohydrate recognition domain in the interaction. The interaction of rat and human SP-D with M. pneumoniae was unaffected by the presence of surfactant lipids and the hydrophobic surfactant proteins. These findings demonstrate that M. pneumoniae is likely to be recognized by SP-D in the alveolar environment and that primary determinants recognized on the organism are lipid components of the cell membrane.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.M201089200
- CiNii Articles
- http://ci.nii.ac.jp/naid/80015380383
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/11916969
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000176204500037&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1074/jbc.M201089200
- ISSN : 0021-9258
- CiNii Articles ID : 80015380383
- PubMed ID : 11916969
- Web of Science ID : WOS:000176204500037