Prediction of three-dimensional structure of Chlamydia trachomatis heat shock protein 60: An immunodominant antigen.

10.5580/131e ◽  
2009 ◽  
Vol 4 (2) ◽  
Keyword(s):  
Heat Shock ◽  
Chlamydia Trachomatis ◽  
Heat Shock Protein ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Heat Shock Protein 60 ◽  
Three Dimensional Structure ◽  
Immunodominant Antigen

scholarly journals Association of Antibodies to Chlamydia trachomatis Heat-Shock Protein 60 kD with Chronic Nongonococcal Urethritis

1997 ◽  
Vol 24 (4) ◽  
pp. 653-660 ◽  
Author(s):  
P. J. Horner ◽  
D. Cain ◽  
M. McClure ◽  
B. J. Thomas ◽  
C. Gilroy ◽  
...  
Keyword(s):  
Heat Shock ◽  
Chlamydia Trachomatis ◽  
Heat Shock Protein ◽  
Heat Shock Protein 60 ◽  
Nongonococcal Urethritis

scholarly journals Heat Shock Protein Genes Undergo Dynamic Alteration in Their Three-Dimensional Structure and Genome Organization in Response to Thermal Stress

2017 ◽  
Vol 37 (24) ◽  
Author(s):  
Surabhi Chowdhary ◽  
Amoldeep S. Kainth ◽  
David S. Gross
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Rna Polymerase Ii ◽  
De Novo ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Chromosome Conformation ◽  
Coding Regions ◽  
Response To Stress

ABSTRACT Three-dimensional (3D) chromatin organization is important for proper gene regulation, yet how the genome is remodeled in response to stress is largely unknown. Here, we use a highly sensitive version of chromosome conformation capture in combination with fluorescence microscopy to investigate Heat Shock Protein (HSP) gene conformation and 3D nuclear organization in budding yeast. In response to acute thermal stress, HSP genes undergo intense intragenic folding interactions that go well beyond 5′-3′ gene looping previously described for RNA polymerase II genes. These interactions include looping between upstream activation sequence (UAS) and promoter elements, promoter and terminator regions, and regulatory and coding regions (gene “crumpling”). They are also dynamic, being prominent within 60 s, peaking within 2.5 min, and attenuating within 30 min, and correlate with HSP gene transcriptional activity. With similarly striking kinetics, activated HSP genes, both chromosomally linked and unlinked, coalesce into discrete intranuclear foci. Constitutively transcribed genes also loop and crumple yet fail to coalesce. Notably, a missense mutation in transcription factor TFIIB suppresses gene looping, yet neither crumpling nor HSP gene coalescence is affected. An inactivating promoter mutation, in contrast, obviates all three. Our results provide evidence for widespread, transcription-associated gene crumpling and demonstrate the de novo assembly and disassembly of HSP gene foci.

scholarly journals Immunization with a Peptide Corresponding to Chlamydial Heat Shock Protein 60 Increases the Humoral Immune Response in C3H Mice to a Peptide Representing Variable Domain 4 of the Major Outer Membrane Protein of Chlamydia trachomatis

1999 ◽  
Vol 6 (3) ◽  
pp. 356-363 ◽  
Author(s):  
Vladimir L. Motin ◽  
Luis M. de la Maza ◽  
Ellena M. Peterson
Keyword(s):  
Immune Response ◽  
Cell Proliferation ◽  
T Cell ◽  
Heat Shock ◽  
Chlamydia Trachomatis ◽  
Membrane Protein ◽  
Heat Shock Protein ◽  
T Cell Proliferation ◽  
Heat Shock Protein 60 ◽  
C3h Mice

ABSTRACT C3H (H-2k ) mice are susceptible to a vaginal challenge with human strains of Chlamydia trachomatis and thus are a useful strain for testing potentialChlamydia vaccine candidates. However, C3H mice are fairly poor responders in terms of the level of antibody resulting from immunization with potential protective peptides representing variable domains (VDs) of the major outer membrane protein (MOMP). C57BL/6 (H-2b ) mice, on the other hand, are moderately resistant to a vaginal challenge but are good responders to the chlamydial MOMP VDs. Peptides representing universal T-cell helper epitopes were employed to determine whether the antibody response to a peptide representing VD4 of the MOMP, which has been shown to contain neutralizing epitopes, could be enhanced in C3H and C57 mice. Universal T-cell helper peptides from tetanus toxin, the pre-S2 region of hepatitis B virus, and the mouse heat shock protein 60, as well as the corresponding segment of the Chlamydia heat shock protein 60 (hspct), were coadministered with the VD4 peptide. Peptides were coencapsulated in liposomes containing the adjuvant monophosphoryl lipid A and administered by using a combination of mucosal and intramuscular injection. The only T-cell helper peptide that improved the immune response as judged by antibody level, in vitro neutralization assays, and T-cell proliferation was hspct. The response in the C57BL/6 strain was not significantly enhanced with hspct over levels achieved with VD4 alone; however, in C3H mice the levels of serum antibody to C. trachomatisincreased to that seen in C57 mice. However, the molecular specificity and immunoglobulin subclass distribution differed from those of the C57 response, and the neutralizing titers and T-cell proliferation responses were lower. In both strains of mice, titers of vaginal antibody to C. trachomatis were low. In summary, of the T-helper peptides used, only hspct significantly enhanced the immune response of C3H mice to the VD4 peptide, but it had only a modest effect on the immune response of C57 mice.

scholarly journals Vaccination with Heat Shock Protein 60 Induces a Protective Immune Response against Experimental Paracoccidioides brasiliensis Pulmonary Infection

2008 ◽  
Vol 76 (9) ◽  
pp. 4214-4221 ◽  
Author(s):  
Renata de Bastos Ascenço Soares ◽  
Francisco J. Gomez ◽  
Célia Maria de Almeida Soares ◽  
George S. Deepe
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Paracoccidioides Brasiliensis ◽  
Humoral Response ◽  
Interleukin 12 ◽  
Heat Shock Protein 60 ◽  
Lethal Challenge ◽  
Immunodominant Antigen ◽  
Ifn Γ

ABSTRACT Paracoccidioides brasiliensis causes a chronic granulomatous mycosis prevalent in Latin America. The successful resolution of infection with this fungus is dependent on the activation of cellular immunity. We previously identified heat shock protein 60 (HSP60) as a target of the humoral response in paracoccidioidomycosis. Herein we expressed the gene encoding HSP60 in Escherichia coli and analyzed the immunological activity of this recombinant antigen. The immunization of BALB/c mice with recombinant protein emulsified in adjuvant stimulated a cellular immune response. Splenocytes from immunized mice proliferated in response to antigen and released interleukin-12 and gamma interferon (IFN-γ). Vaccination with HSP60 reduced the fungal burden in mice given 106 or 107 yeasts and protected mice from a lethal challenge. The efficacy of the vaccination was blunted by the neutralization of IFN-γ. CD4+ cells were necessary for the efficacy of the vaccination in both the afferent and efferent phases. Thus, we have demonstrated that this immunodominant antigen is a candidate for the development of a vaccine against this fungus.

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Nature ◽  
1990 ◽  
Vol 346 (6285) ◽  
pp. 623-628 ◽  
Author(s):  
Kevin M. Flaherty ◽  
Camilla DeLuca-Flaherty ◽  
David B. McKay
Keyword(s):  
Heat Shock ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Heat Shock Cognate Protein ◽  
Cognate Protein
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