A protective domain of heat-shock protein 60 from Histoplasma capsulatum

Journal of Infectious Diseases

Volumn 174, Issue 4, 1996, Pages 828-834

  Deepe Jr , George S ^a   Gibbons, Reta ^a   Brunner, George D ^a   Gomez, Francisco J ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN RECOGNITION; ANTIGENICITY; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; HISTOPLASMA CAPSULATUM; IMMUNE RESPONSE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; RECOMBINANT DNA TECHNOLOGY; SPLEEN CELL; VACCINATION;

EID: 19244361902     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1093/infdis/174.4.828     Document Type: Article

References (15)

1. Garcia JP, Howard DU. Characterization of antigens from the yeast phase of Histoplasma capsiilalum. Infect Immun 1971;4:116-25.
2. Feit C, Tewari RP. Immunogenicity of ribosomal preparations of yeast cells of Histoplasma capsulalum. Infect Immun 1974;5:1091-7.
3. Gomez AM, Rhodes JC, Deepe GS Jr. Antigenicity and immunogenicity of an extract from the cell wall and cell membrane of Histoplasma capsulation yeast cells. Infect Immun 1991;59:330-6.
4. Gomez FJ, Gomez AM, Deepe GS Jr. Protective efficacy of a 62-kilodalton antigen, HIS-62, from the cell wall and cell membrane of Histoplasma capsulatum yeast cells. Infect Immun 1991;59:4459-64.
5. Gomez FJ, Allendoerfer R, Deepe GS Jr. Vaccination with recombinant heat shock protein 60 from Histoplasma capsulatum protects mice against pulmonary histoplasmosis. Infect Immun 1995;63:2587-95.
6. Bradford MM. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
7. Rothman JE. Polypeptide chain binding properties: catalysts of protein folding and related processes in cells. Cell 1989;59:591-601.
8. Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992;355:33-45.
9. Koll HB, Guiard B, Rassow J, et al. Antifolding activity of hsp 60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 1992;68:1163-75.
10. Young DB, Lathigra R, Hendrix R, Sweetser D, Young RA. Stress proteins are immune targets in leprosy and tuberculosis. Proc Natl Acad Sci USA 1988;85:4267-70.
11. Morrison RP, Belland RJ, Lyng K, Caldwell HD. Chlamydial disease pathogenesfs: the 57-kD chlamydial hypersensitivity antigen is a stress protein. J Exp Med 1989;170:1271-83.
12. Blander SJ, Horowitz MA. Major cytoplasmic membrane protein of Legionella pneumophila, a genus common antigen and member of the hsp 60 family of heat shock proteins, induces protective immunity in a guinea pig model of Legionnaire's disease. J Clin Invest 1993;91:717-23.
13. Deepe GS Jr, Bullock WE. Histoplasmosis: a granulomatous inflammatory response. In: Gallin JI, Goldstein IM, Synderman R, eds. Inflammation: basic principles and clinical practices. 2nd ed. New York: Raven Press, 1992:943-58.
14. Germain RN. Antigen processing and presentation. In: Paul WE, ed. Fundamental immunology. 3rd ed. New York: Raven Press, 1993:629-76.
15. Lussow AR, Barrios C, van Embden J, et al. Mycobacterial heat-shock proteins as carrier molecules. Eur J Immunol 1991;21:2297-302.