2005
DOI: 10.1016/j.febslet.2005.11.060
|View full text |Cite
|
Sign up to set email alerts
|

Heat shock protein 60: Identification of specific epitopes for binding to primary macrophages

Abstract: In the present study, we characterized regions of human heat shock protein (HSP) 60 responsible for binding to primary macrophages. Studies using 20-mer peptides of the HSP60 sequence to compete with HSP60-binding to macrophages from C57BL/6J mice showed that regions aa241-260, aa391-410 and aa461-480 are involved in surface-binding. HSP60 mutants, lacking the N-terminal 137, 243 or 359 amino acids, inhibited HSP60-binding to primary macrophages to different degrees, demonstrating that all three regions are re… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

1
28
0
1

Year Published

2007
2007
2017
2017

Publication Types

Select...
5
4

Relationship

0
9

Authors

Journals

citations
Cited by 48 publications
(30 citation statements)
references
References 34 publications
1
28
0
1
Order By: Relevance
“…In case there was binding of Hsp60 via surface receptors, the expected consequence would be activation of CD68-positive cells followed by inflammatory response, as shown in the in vitro models. [49][50][51] All together, these results support the working hypothesis that Hsp60 can play a decisive role in the pathogenesis of UC, and make Hsp60 a promising candidate for the treatment of UC with antichaperonin agents.…”
Section: Discussionsupporting
confidence: 71%
“…In case there was binding of Hsp60 via surface receptors, the expected consequence would be activation of CD68-positive cells followed by inflammatory response, as shown in the in vitro models. [49][50][51] All together, these results support the working hypothesis that Hsp60 can play a decisive role in the pathogenesis of UC, and make Hsp60 a promising candidate for the treatment of UC with antichaperonin agents.…”
Section: Discussionsupporting
confidence: 71%
“…This can be proven by following facts: their availability in both eukaryotic and prokaryotic organisms; presence of highly conserved sequences in the structure of HSP, which are also immunodominant; high immunologic activity of HSP. The HSPdependent system (network) of inflammation and autoimmu nity stimulation and regulation includes, at any rate, following elements: HSP as polyreactive antigens; natural auto antibodies and anti-idiotypic antibodies; proteins of macro organism as such released from the cells due to various reasons; foreign proteins (including HSP of microorganisms); antigen-presenting cells that can be activated by HSP; effector and regulatory T-lymphocytes interacting with HSP [12][13][14][15].…”
Section: Resultsmentioning
confidence: 99%
“…In view of several particulars of formation of B-cell response to heat shock proteins [12][13][14][15], as well as reports on potential effects of antiidiotypic serum antibodies on the nature of immunochemical reactions (e.g. socalled prozone effect in tests based on agglutination or precipitation reaction) [16][17][18]; additionally, development of indirect ELISA for identification of anti-HSP-60 IgG-antibodies using biotinylated tyramine reagent was performed.…”
Section: Resultsmentioning
confidence: 99%
“…The vaccination of mice with Hsp60 confers protection from Histoplasma through both cellular (CD4 ϩ T cells [7]) and humoral immune mechanisms (11). In addition, Hsp60 can function as an adhesin for yeast binding to complement receptors on host macrophages (12,19). Indicating the importance of ameliorating heat stresses, virulence differences among Histoplasma strains are correlated with in vitro thermosensitivity and differences in heat shock response (5).…”
mentioning
confidence: 99%