This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
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 Cloud-Hansen, K. A.
Right arrow Articles by Dillard, J. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cloud-Hansen, K. A.
Right arrow Articles by Dillard, J. P.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2008, p. 5989-5994, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00506-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Neisseria gonorrhoeae Uses Two Lytic Transglycosylases To Produce Cytotoxic Peptidoglycan Monomers{triangledown} ,{dagger}

Karen A. Cloud-Hansen, Kathleen T. Hackett, Daniel L. Garcia, and Joseph P. Dillard*

Department of Medical Microbiology and Immunology, University of Wisconsin—Madison School of Medicine and Public Health, Madison, Wisconsin 53706

Received 14 April 2008/ Accepted 12 June 2008

Peptidoglycan fragments released by Neisseria gonorrhoeae contribute to the inflammation and ciliated cell death associated with gonorrhea and pelvic inflammatory disease. However, little is known about the production and release of these fragments during bacterial growth. Previous studies demonstrated that one lytic transglycosylase, LtgA, was responsible for the production of approximately half of the released peptidoglycan monomers. Systematic mutational analysis of other putative lytic transglycosylase genes identified lytic transglycosylase D (LtgD) as responsible for release of peptidoglycan monomers from gonococci. An ltgA ltgD double mutant was found not to release peptidoglycan monomers and instead released large, soluble peptidoglycan fragments. In pulse-chase experiments, recycled peptidoglycan was not found in cytoplasmic extracts from the ltgA ltgD mutant as it was for the wild-type strain, indicating that generation of anhydro peptidoglycan monomers by lytic transglycosylases facilitates peptidoglycan recycling. The ltgA ltgD double mutant showed no growth abnormalities or cell separation defects, suggesting that these enzymes are involved in pathogenesis but not necessary for normal growth.

* Corresponding author. Mailing address: 1550 Linden Drive, 6301 Microbial Sciences Building, Madison, WI 53706. Phone: (608) 265-2837. Fax: (608) 262-8418. E-mail: jpdillard{at}wisc.edu

{triangledown} Published ahead of print on 20 June 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, September 2008, p. 5989-5994, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00506-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Adin, D. M., Engle, J. T., Goldman, W. E., McFall-Ngai, M. J., Stabb, E. V. (2009). Mutations in ampG and Lytic Transglycosylase Genes Affect the Net Release of Peptidoglycan Monomers from Vibrio fischeri. J. Bacteriol. 191: 2012-2022 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»