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
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 Putnoky, P.
Right arrow Articles by Kerepesi, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Putnoky, P.
Right arrow Articles by Kerepesi, I.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2004, p. 1591-1597, Vol. 186, No. 6
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.6.1591-1597.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

H Protein of Bacteriophage 16-3 and RkpM Protein of Sinorhizobium meliloti 41 Are Involved in Phage Adsorption

Péter Putnoky,* Veronika Deák, Krisztina Békási, Adrienn Pálvölgyi, Anita Maász, Zsuzsanna Palágyi, Gyula Hoffmann, and Ildikó Kerepesi

Department of Genetics and Molecular Biology, Faculty of Sciences, University of Pécs, H-7601 Pécs, Hungary

Received 4 August 2003/ Accepted 2 December 2003

The strain-specific capsular polysaccharide KR5 antigen of Sinorhizobium meliloti 41 is required both for invasion of the symbiotic nodule and for the adsorption of bacteriophage 16-3. In order to know more about the genes involved in these events, bacterial mutants carrying an altered phage receptor were identified by using host range phage mutants. A representative mutation was localized in the rkpM gene by complementation and DNA sequence analysis. A host range phage mutant isolated on these phage-resistant bacteria was used to identify the h gene, which is likely to encode the tail fiber protein of phage 16-3. The nucleotide sequences of the h gene as well as a host range mutant allele were also established. In both the bacterial and phage mutant alleles, a missense mutation was found, indicating a direct contact between the RkpM and H proteins in the course of phage adsorption. Some mutations could not be localized in these genes, suggesting that additional components are also important for bacteriophage receptor recognition.

* Corresponding author. Mailing address: Department of Genetics and Molecular Biology, University of Pécs, P.O. Box 266, H-7601 Pécs, Hungary. Phone: 36 (72) 503 600. Fax: 36 (72) 501 527. E-mail: putnoky{at}ttk.pte.hu.

Journal of Bacteriology, March 2004, p. 1591-1597, Vol. 186, No. 6
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.6.1591-1597.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Le Quere, A. J.-L., Deakin, W. J., Schmeisser, C., Carlson, R. W., Streit, W. R., Broughton, W. J., Forsberg, L. S. (2006). Structural Characterization of a K-antigen Capsular Polysaccharide Essential for Normal Symbiotic Infection in Rhizobium sp. NGR234: DELETION OF THE rkpMNO LOCUS PREVENTS SYNTHESIS OF 5,7-DIACETAMIDO-3,5,7,9-TETRADEOXY-NON-2-ULOSONIC ACID. J. Biol. Chem. 281: 28981-28992 [Abstract] [Full Text]  
  • Duplessis, M., Levesque, C. M., Moineau, S. (2006). Characterization of Streptococcus thermophilus Host Range Phage Mutants. Appl. Environ. Microbiol. 72: 3036-3041 [Abstract] [Full Text]  
  • Ferenczi, S., Orosz, L., Papp, P. P. (2006). Repressor of Phage 16-3 with Altered Binding Specificity Indicates Spatial Differences in Repressor-Operator Complexes. J. Bacteriol. 188: 1663-1666 [Abstract] [Full Text]  
  • Ganyu, A., Csiszovszki, Z., Ponyi, T., Kern, A., Buzas, Z., Orosz, L., Papp, P. P. (2005). Identification of Cohesive Ends and Genes Encoding the Terminase of Phage 16-3. J. Bacteriol. 187: 2526-2531 [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»