This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ASM journals
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cheng, Q.
Right arrow Articles by Fischetti, V. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cheng, Q.
Right arrow Articles by Fischetti, V. A.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, January 2005, p. 111-117, Vol. 49, No. 1
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.1.111-117.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Removal of Group B Streptococci Colonizing the Vagina and Oropharynx of Mice with a Bacteriophage Lytic Enzyme

Qi Cheng, Daniel Nelson, Shiwei Zhu, and Vincent A. Fischetti*

Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York

Received 7 June 2004/ Returned for modification 6 August 2004/ Accepted 22 September 2004

Group B streptococci (GBS) are the leading cause of neonatal meningitis and sepsis worldwide. The current treatment strategy is limited to intrapartum antibiotic prophylaxis in pregnant women to prevent early-onset neonatal diseases, but considering the potential for antibiotic resistance, the risk of losing control over the disease is high. To approach this problem, we have developed a bacteriophage (phage) lytic enzyme to remove colonizing GBS. Bacteriophage muralytic enzymes, termed lysins, are highly evolved molecules designed to degrade the cell wall of host bacteria to release phage particles from the bacterial cytoplasm. Several different lysins have been developed to specifically kill bacterial pathogens both on mucosal surfaces and in blood and represent a novel approach to control infection. A lysin cloned from a phage infecting GBS was found to contain two putative catalytic domains and one putative binding domain, which is similar to the domain organization of some staphylococcal phage lysins. The lysin (named PlyGBS) was recombinantly expressed in Escherichia coli, and purified PlyGBS efficiently killed all tested GBS serotypes in vitro. In a mouse model, a single dose of PlyGBS significantly reduced bacterial colonization in both the vagina and oropharynx. As an alternative strategy for intrapartum antibiotic prophylaxis, this approach may be used to reduce vaginal GBS colonization in pregnant women before delivery or to decontaminate newborns, thus reducing the incidence of GBS-associated neonatal meningitis and sepsis.


* Corresponding author. Mailing address: Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, 1230 York Ave., New York, NY 10021. Phone: (212) 327-8166. E-mail: vaf{at}rockefeller.edu.


Antimicrobial Agents and Chemotherapy, January 2005, p. 111-117, Vol. 49, No. 1
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.1.111-117.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Daniel, A., Euler, C., Collin, M., Chahales, P., Gorelick, K. J., Fischetti, V. A. (2010). Synergism between a Novel Chimeric Lysin and Oxacillin Protects against Infection by Methicillin-Resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 54: 1603-1612 [Abstract] [Full Text]  
  • Oey, M., Lohse, M., Scharff, L. B., Kreikemeyer, B., Bock, R. (2009). Plastid production of protein antibiotics against pneumonia via a new strategy for high-level expression of antimicrobial proteins. Proc. Natl. Acad. Sci. USA 106: 6579-6584 [Abstract] [Full Text]  
  • Horgan, M., O'Flynn, G., Garry, J., Cooney, J., Coffey, A., Fitzgerald, G. F., Ross, R. P., McAuliffe, O. (2009). Phage Lysin LysK Can Be Truncated to Its CHAP Domain and Retain Lytic Activity against Live Antibiotic-Resistant Staphylococci. Appl. Environ. Microbiol. 75: 872-874 [Abstract] [Full Text]  
  • Pritchard, D. G., Dong, S., Kirk, M. C., Cartee, R. T., Baker, J. R. (2007). LambdaSa1 and LambdaSa2 Prophage Lysins of Streptococcus agalactiae. Appl. Environ. Microbiol. 73: 7150-7154 [Abstract] [Full Text]  
  • Samen, U., Eikmanns, B. J., Reinscheid, D. J., Borges, F. (2007). The Surface Protein Srr-1 of Streptococcus agalactiae Binds Human Keratin 4 and Promotes Adherence to Epithelial HEp-2 Cells. Infect. Immun. 75: 5405-5414 [Abstract] [Full Text]  
  • Baker, J. R., Liu, C., Dong, S., Pritchard, D. G. (2006). Endopeptidase and Glycosidase Activities of the Bacteriophage B30 Lysin. Appl. Environ. Microbiol. 72: 6825-6828 [Abstract] [Full Text]  
  • Donovan, D. M., Foster-Frey, J., Dong, S., Rousseau, G. M., Moineau, S., Pritchard, D. G. (2006). The Cell Lysis Activity of the Streptococcus agalactiae Bacteriophage B30 Endolysin Relies on the Cysteine, Histidine-Dependent Amidohydrolase/Peptidase Domain. Appl. Environ. Microbiol. 72: 5108-5112 [Abstract] [Full Text]  
  • Donovan, D. M., Dong, S., Garrett, W., Rousseau, G. M., Moineau, S., Pritchard, D. G. (2006). Peptidoglycan Hydrolase Fusions Maintain Their Parental Specificities. Appl. Environ. Microbiol. 72: 2988-2996 [Abstract] [Full Text]  
  • Yoong, P., Schuch, R., Nelson, D., Fischetti, V. A. (2006). PlyPH, a Bacteriolytic Enzyme with a Broad pH Range of Activity and Lytic Action against Bacillus anthracis. J. Bacteriol. 188: 2711-2714 [Abstract] [Full Text]  
  • Borysowski, J., Weber-Dabrowska, B., Gorski, A. (2006). Bacteriophage Endolysins as a Novel Class of Antibacterial Agents. Exp Biol Med 231: 366-377 [Abstract] [Full Text]  
  • Delisle, A. L., Barcak, G. J., Guo, M. (2006). Isolation and Expression of the Lysis Genes of Actinomyces naeslundii Phage Av-1. Appl. Environ. Microbiol. 72: 1110-1117 [Abstract] [Full Text]