Protein D expression promotes the adherence and internalization of non-typeable Haemophilus influenzae into human monocytic cells

被引:49
作者
Ahrén, IL [1 ]
Janson, H [1 ]
Forsgren, A [1 ]
Riesbeck, K [1 ]
机构
[1] Lund Univ, Dept Med Microbiol, Malmo Univ Hosp, S-20502 Malmo, Sweden
关键词
non-typeable Haemophilus influenzae; internalization; glycerophosphodiester phosphodiesterase; protein D; monocytes;
D O I
10.1006/mpat.2001.0456
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Protein D, having a glycerol-3-phosphodiester phosphodiesterase activity, is found at the surface of all Haemophilus influenzae strains and is a possible virulence factor. In the present study, the involvement of protein D in the entry of NTHi into human monocytic cells is reported. Primary monocytes and the monocytic cell lines U-937 and THP-1 were infected with NTHi strain 772 and the mutant 772 Delta hpd1 (lacking the gene for protein D). NTHi 772 adhered to and entered monocytic cells up to four-fold more efficiently compared to 772 Delta hpd1. When an Escherichia coli transformant expressing protein D was incubated with monocytic cells, the number of intracellular bacteria increased 1.6-fold compared to protein D-deficient controls. Any correlation between internalization and phosphorylcholine expression was not detected. In conclusion, our data suggest that surface-expressed protein D promotes the adherence of NTHi to human monocytes leading to a higher number of internalized bacteria. (C) 2001 Academic Press.
引用
收藏
页码:151 / 158
页数:8
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