Identification of the amino acid residues critical for specific binding of the bacteriolytic enzyme of γ-phage, PlyG, to Bacillus anthracis

Biochemical and Biophysical Research Communications

Volumn 363, Issue 3, 2007, Pages 531-535

  Kikkawa, Hitomi ^a   Fujinami, Yoshihito ^a,b   Suzuki, Shin ichi ^a   Yasuda, Jiro ^a,b  

^a NATIONAL RESEARCH INSTITUTE OF POLICE SCIENCE   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

phage; Bacillus anthracis; Binding domain; Mutational analysis; N Acetylmuramoyl l alanine amidase; PlyG

Indexed keywords

ALANINE; AMINO ACID; PLYG PROTEIN; UNCLASSIFIED DRUG; VIRUS ENZYME;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS ANTHRACIS; BACTERIOLYSIS; BACTERIOPHAGE; BACTERIUM DETECTION; BETA SHEET; BINDING SITE; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME SPECIFICITY; MUTATIONAL ANALYSIS; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; AMINO ACIDS; BACILLUS ANTHRACIS; BACILLUS PHAGES; BACTERIOLYSIS; BINDING SITES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID; VIRAL PROTEINS;

BACILLUS ANTHRACIS;

EID: 34848846560     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.09.002     Document Type: Article

References (27)

1. Nicholson W.L., and Galeano B. UV resistance of Bacillus anthracis spores revisited: validation of Bacillus subtilis spores as UV surrogates for spores of B. anthracis Sterne,. Appl. Environ. Microbiol. 69 (2003) 1327-1330
2. Molnar J., and Pragai B. Attempts to detect the presence of teichoic acid in Bacillus anthracis. Acta Microbiol. Acad. Sci. Hung. 18 (1971) 105-108
3. Mock M., and Fouet A. Anthrax. Annu. Rev. Microbiol. 55 (2001) 647-671
4. Turnbull P.C.B., and Kramer J.M. Bacillus. In: Murray P.R., Baron M.A., Tenover F.C., and Yolken R.H. (Eds). Manual of clinical microbiology. sixth ed. (1995), ASM Press, Washington, D.C. 349-356
5. Keim P., Smith K.L., Keys C., Takahashi H., Kurata T., and Kaufmann A. Molecular investigation of the Aum Shinrikyo anthrax release in Kameido, Japan. J. Clin. Microbiol. 39 (2001) 4566-4567
6. Inglesby T.V., O'Toole T., Henderson D.A., Bartlett J.G., Ascher M.S., Eitzen E., Friedlander A.M., Gerberding J., Hauer J., Hughes J., McDade J., Osterholm M.T., Parker G., Perl T.M., Russell P.K., and Tonat K. Anthrax as a biological weapon, 2002: updated recommendations for management. JAMA 287 (2002) 2236-2252
7. Higgins J.A., Cooper M., Schroeder-Tucker L., Black S., Miller D., Karns J.S., Manthey E., Breeze R., and Perdue M.L. A field investigation of Bacillus anthracis contamination of U.S. Department of Agriculture and other Washington, D.C., buildings during the anthrax attack of October 2001. Appl. Environ. Microbiol. 69 (2003) 593-599
8. BROWN E.R., and Cherry W. Specific identification of Bacillus anthracis by means of a variant bacteriophage. J. Infect. Dis. 96 (1955) 34-39
9. Young R. Bacteriophage lysis: mechanism and regulation. Microbial. Rev. 56 (1992) 430-481
10. Schuch R., Nelson D., and Fischetti V.A. A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 418 (2002) 884-889
11. Loessner M.J., Maier S.K., Daubek-Puza H., Wendlinger G., and Scherer S. Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli. J. Bacteriol. 179 (1997) 2845-2851
12. Shida T., Hattori H., Ise F., and Sekiguchi J. Mutational analysis of catalytic sites of the cell wall lytic N-acetylmuramoyl-l-alanine amidases CwlC and CwlV. J. Biol. Chem. 276 (2001) 28140-28146
13. Low L.Y., Yang C., Perego M., Osterman A., and Liddington R.C. Structure and lytic activity of a Bacillus anthracis prophage endolysin. J. Biol. Chem. 280 (2005) 35433-35439
14. Loessner M.J., Kramer K., Ebel F., and Scherer S. C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 44 (2002) 335-349
15. Korndorfer I.P., Danzer J., Schmelcher M., Zimmer M., Skerra A., and Loessner M.J. The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls. J. Mol. Biol. 364 (2006) 678-689
16. Fujinami Y., Hirai Y., Sakai I., Yoshino M., and Yasuda J. Sensitive detection of Bacillus anthracis using a binding protein originating from gamma-phage. Microbiol. Immunol. 51 (2007) 163-169
17. Ghuysen J.M., Lamotte-Brasseur J., Joris B., and Shockman G.D. Binding site-shaped repeated sequences of bacterial wall peptidoglycan hydrolases. FEBS Lett. 342 (1994) 23-28
18. Bateman A., and Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J. Mol. Biol. 299 (2000) 1113-1119
19. Kobe B., and Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11 (2001) 725-732
20. Milohanic E., Jonquieres R., Cossart P., Berche P., and Gaillard J.L. The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor. Mol. Microbiol. 39 (2001) 1212-1224
21. Romero P., Lopez R., and Garcia E. Characterization of LytA-like N-acetylmuramoyl-l-alanine amidases from two new Streptococcus mitis bacteriophages provides insights into the properties of the major pneumococcal autolysin. J. Bacteriol. 186 (2004) 8229-8239
22. Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., and Kojima C. Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. Biochemistry 44 (2005) 10153-10163
23. Yoong P., Schuch R., Nelson D., and Fischetti V.A. PlyPH, a bacteriolytic enzyme with a broad pH range of activity and lytic action against Bacillus anthracis. J. Bacteriol. 188 (2006) 2711-2714
24. Dang J.L., Heroux K., Kearney J., Arasteh A., Gostomski M., and Emanuel P.A. Bacillus spore inactivation methods affect detection assays. Appl. Environ. Microbiol. 67 (2001) 3665-3670
25. Ackermann H.W., Roy R., Martin M., Murthy M.R., and Smirnoff W.A. Partial characterization of a cubic Bacillus phage. Can. J. Microbiol. 24 (1978) 986-993
26. Krogh S., Jorgensen S.T., and Devine K.M. Lysis genes of the Bacillus subtilis defective prophage PBSX. J. Bacteriol. 180 (1998) 2110-2117
27. Birdsell D.C., Hathaway G.M., and Rutberg L. Characterization of temperate Bacillus bacteriophage phi105. J. Virol. 4 (1969) 264-270