Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis
作者： Dennis E. Lopatin , Eduardo Jaramillo , Chris A. Edwards , Neal Poperin , Allison Combs
DOI: 10.1111/J.1574-6968.1999.TB08820.X
关键词:
摘要: We previously reported an association between elevated serum antibody titers to the 90-kDa human heat shock protein (Hsp90), periodontal health and colonization by Porphyromonas gingivalis. In this study, we examined cellular localization of Hsp90 homologue P. Cultures gingivalis were heat-stressed (45°C) for homologue. Heat stress induced a 4–5-fold increase in anti-Hsp90 reactivity over that unstressed controls. Western blot analysis revealed two bands (44 68 kDa) reacted with antibodies. The 68-kDa band was heat-inducible, while 44-kDa not. Immunogold staining localized principally membrane extracellular vesicles. Subcellular fractionation confirmed primarily membrane-associated.
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sci-hub.se 参考文章(21)
T Rowland, R C Matthews, F Walton, J P Burnie, D Howat, Autoantibody to heat-shock protein 90 can mediate protection against systemic candidosis. Immunology. ,vol. 74, pp. 20- 24 ,(1991)
E. Craig, J. C A Bardwell, M. Zylicz, C. Georgopoulos, J. King, K. Tilly, The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein. Journal of Biological Chemistry. ,vol. 261, pp. 1782- 1785 ,(1986) , 10.1016/S0021-9258(17)36008-8
T E Bramanti, S C Holt, Localization of a Porphyromonas gingivalis 26-kilodalton heat-modifiable, hemin-regulated surface protein which translocates across the outer membrane. Journal of Bacteriology. ,vol. 174, pp. 5827- 5839 ,(1992) , 10.1128/JB.174.18.5827-5839.1992
R C Matthews, J P Burnie, S Tabaqchali, Isolation of immunodominant antigens from sera of patients with systemic candidiasis and characterization of serological response to Candida albicans. Journal of Clinical Microbiology. ,vol. 25, pp. 230- 237 ,(1987) , 10.1128/JCM.25.2.230-237.1987
M Ensgraber, M Loos, A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infection and Immunity. ,vol. 60, pp. 3072- 3078 ,(1992) , 10.1128/IAI.60.8.3072-3078.1992
Ann Progulske-Fox, Somying Tumwasorn, Stanley C. Holt, The expression and function of a Bacteroides gingivalis hemagglutinin gene in Escherichia coll Oral Microbiology and Immunology. ,vol. 4, pp. 121- 131 ,(1989) , 10.1111/J.1399-302X.1989.TB00238.X
K. Liberek, C. Georgopoulos, M. Zylicz, Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication Proceedings of the National Academy of Sciences of the United States of America. ,vol. 85, pp. 6632- 6636 ,(1988) , 10.1073/PNAS.85.18.6632
D. Hinode, R. Nakamura, D. Grenier, D. Mayrand, Cross‐reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria of human origin Oral Microbiology and Immunology. ,vol. 13, pp. 55- 58 ,(1998) , 10.1111/J.1399-302X.1998.TB00752.X
M.-F. Weidner, D. Grenier, D. Mayrand, Proteolytic artifacts in SDS‐PAGE analysis of selected periodontal pathogen: Oral Microbiology and Immunology. ,vol. 11, pp. 103- 108 ,(1996) , 10.1111/J.1399-302X.1996.TB00343.X
H. K. Mitchell, N. S. Petersen, C. H. Buzin, Self-degradation of heat shock proteins. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 82, pp. 4969- 4973 ,(1985) , 10.1073/PNAS.82.15.4969