The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain

Applied and Environmental Microbiology

Volumn 72, Issue 7, 2006, Pages 5108-5112

  Donovan, David M ^a   Foster Frey, Juli ^a   Dong, Shengli ^b   Rousseau, Geneviève M ^c   Moineau, Sylvain ^c   Pritchard, David G ^b  

^a U S DEPARTMENT OF AGRICULTURE   (United States)

^b UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^c UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYME KINETICS; ENZYMES; MICROBIOLOGY; MUTAGENESIS;

CELL LYSIS ACTIVITY; HISTIDINE-DEPENDENT AMIDOHYDROLASE; PEPTIDASE DOMAIN; STREPTOCOCCUS AGALACTIAE BACTERIOPHAGE B30 ENDOLYSIN;

CELLS;

AMIDASE; CYSTEINE; GLYCOSIDASE; HISTIDINE; PEPTIDASE;

BACTERIUM; CELLS AND CELL COMPONENTS; LYSIS;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE; CARBOXY TERMINAL SEQUENCE; CYTOLYSIS; ENZYME ACTIVITY; MASTITIS; NONHUMAN; POINT MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PROTEIN DOMAIN; STREPTOCOCCUS AGALACTIAE; TURBIDITY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CYSTEINE; ENDOPEPTIDASES; HISTIDINE; LYSOGENY; MASTITIS, BOVINE; PEPTIDE HYDROLASES; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS PHAGES;

STREPTOCOCCUS AGALACTIAE;

EID: 33746061682     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.03065-05     Document Type: Article

References (23)

1. Bateman, A., and N. D. Rawlings. 2003. The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem. Sci. 28:234-237.
2. Bolotin, A., P. Wincker, S. Mauger, O. Jaillon, K. Malarme, J. Weissenbach, S. D. Ehrlich, and A. Sorokin. 2001. The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403. Genome Res. 11:731-753.
3. Cheng, Q., D. Nelson, S. Zhu, and V. A. Fischetti. 2005. Removal of group B streptococci colonizing the vagina and oropharynx of mice with a bacteriophage lytic enzyme. Antimicrob. Agents Chemother. 49:111-117.
4. Cohen, M. L. 2000. Changing patterns of infectious disease. Nature 406:762-767.
5. De Oliveira, A. P., J. L. Watts, S. A. Salmon, and F. M. Aarestrup. 2000. Antimicrobial susceptibility of Staphylococcus aureus isolated from bovine mastitis in Europe and the United States. J. Dairy Sci. 83:855-862.
6. Donovan, D. M., D. E. Kerr, and R. J. Wall. 2005. Engineering disease resistant cattle. Transgenic Res. 14:563-567.
7. Donovan, D. M., S. Dong, G. Garrett, G. M. Rousseau, S. Moineau, and D. G. Pritchard. 2006. Peptidoglycan hydrolase fusions maintain their parental specificities. Appl. Environ. Microbiol. 72:2988-2996.
8. Huard, C., G. Miranda, F. Wessner, A. Bolotin, J. Hansen, S. J. Foster, and M. P. Chapot-Chartier. 2003. Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. Microbiology 149:695-705.
9. Kerr, D. E., and O. Wellnitz. 2003. Mammary expression of new genes to combat mastitis. J. Anim. Sci. 81(Suppl. 3):38-47.
10. Pace, C. N., R. W. Alston, and K. L. Shaw. 2000. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9:1395-1398.
11. Ponting, C. P., L. Aravind, J. Schultz, P. Bork, and E. V. Koonin. 1999. Eukaryotic signaling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289:729-745.
12. Pritchard, D. G., S. Dong, J. R. Baker, and J. A. Engler. 2004. The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30. Microbiology 150:2079-2087.
13. Quessy, S., J. D. Dubreuil, M. Caya, and R. Higgins. 1995. Discrimination of virulent and avirulent Streptococcus suis capsular type 2 isolates from different geographical origins. Infect. Immun. 63:1975-1979.
14. Rajala-Schultz, P. J., K. L. Smith, J. S. Hogan, and B. C. Love. 2004. Antimicrobial susceptibility of mastitis pathogens from first lactation and older cows. Vet. Microbiol. 102:33-42.
15. Rigden, D. J., M. J. Jedrzejas, and M. Y. Galperin. 2003. Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate- specific amidohydrolases. Trends Biochem. Sci. 28:230-234.
16. Saxelin, M.-L., E.-L. Nurmiaho-Lassila, V. T. Meriläinen, and R. I. Forsén. 1986. Ultrastructure and host specificity of bacteriophages of Streptococcus cremoris, Streptococcus lactis subsp. diacetylactis, and Leuconostoc cremoris from Finnish fermented milk "viili." Appl. Environ. Microbiol. 52:771-777.
17. Sozzi, T., J. M. Poulin, R. Maret, and R. Pousaz. 1978. Isolation of a bacteriophage of Leuconostoc mesenteroides from dairy products. J. Appl. Bacteriol. 44:159-161.
18. Thiel, K. 2004. Old dogma, new tricks-21st century phage therapy. Nat. Biotechnol. 22:31-36.
19. Tremblay, D. M., and S. Moineau. 1999. Complete genomic sequence of the lytic bacteriophage DT1 of Streptococcus thermophilus. Virology 255:63-76.
20. Van den Heever, L. W., and W. H. Giesecke. 1980. Experimental induction of bovine mastitis with human strains of group B streptococci (Streptococcus agalactiae). J. S. Afr. Vet. Assoc. 51:107-109.
21. Wall, R. J., A. M. Powell, M. J. Paape, D. E. Kerr, D. D. Bannerman, V. G. Pursel, K. D. Wells, N. Talbot, and H. W. Hawk. 2005. Genetically enhanced cows resist intramammary Staphylococcus aureus infection. Nat. Biotechnol. 23:445-451.
22. Whisstock, J. C., and A. M. Lesk. 1999. SH3 domains in prokaryotes. Trends Biochem. Sci. 24:132-133.
23. Yow, M. D., L. J. Leeds, P. K. Thompson, E. O. Mason, Jr., D. J. Clark, and C. W. Beachler. 1980. The natural history of group B streptococcal colonization in the pregnant woman and her offspring. I. Colonization studies. Am. J. Obstet. Gynecol. 137:34-38.