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Applied and Environmental Microbiology, August 2002, p. 3969-3977, Vol. 68, No. 8
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.8.3969-3977.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

A Single Ala139-to-Glu Substitution in the Renibacterium salmoninarum Virulence-Associated Protein p57 Results in Antigenic Variation and Is Associated with Enhanced p57 Binding to Chinook Salmon Leukocytes

Gregory D. Wiens,1* Ron Pascho,2 and James R. Winton2

Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, Oregon 97201,1 Western Fisheries Research Center, Seattle, Washington 981152

Received 29 January 2002/ Accepted 14 May 2002

The gram-positive bacterium Renibacterium salmoninarum produces relatively large amounts of a 57-kDa protein (p57) implicated in the pathogenesis of salmonid bacterial kidney disease. Antigenic variation in p57 was identified by using monoclonal antibody 4C11, which exhibited severely decreased binding to R. salmoninarum strain 684 p57 and bound robustly to the p57 proteins of seven other R. salmoninarum strains. This difference in binding was not due to alterations in p57 synthesis, secretion, or bacterial cell association. The molecular basis of the 4C11 epitope loss was determined by amplifying and sequencing the two identical genes encoding p57, msa1 and msa2. The 5' and coding sequences of the 684 msa1 and msa2 genes were identical to those of the ATCC 33209 msa1 and msa2 genes except for a single C-to-A nucleotide mutation. This mutation was identified in both the msa1 and msa2 genes of strain 684 and resulted in an Ala139-to-Glu substitution in the amino-terminal region of p57. We examined whether this mutation in p57 altered salmonid leukocyte and rabbit erythrocyte binding activities. R. salmoninarum strain 684 extracellular protein exhibited a twofold increase in agglutinating activity for chinook salmon leukocytes and rabbit erythrocytes compared to the activity of the ATCC 33209 extracellular protein. A specific and quantitative p57 binding assay confirmed the increased binding activity of 684 p57. Monoclonal antibody 4C11 blocked the agglutinating activity of the ATCC 33209 extracellular protein but not the agglutinating activity of the 684 extracellular protein. These results indicate that the Ala139-to-Glu substitution altered immune recognition and was associated with enhanced biological activity of R. salmoninarum 684 p57.

* Corresponding author. Mailing address: Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97201. Phone: (503) 494-7718. Fax: (503) 494-6862. E-mail: wiensg{at}ohsu.edu.

Applied and Environmental Microbiology, August 2002, p. 3969-3977, Vol. 68, No. 8
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.8.3969-3977.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wiens, G. D., Rockey, D. D., Wu, Z., Chang, J., Levy, R., Crane, S., Chen, D. S., Capri, G. R., Burnett, J. R., Sudheesh, P. S., Schipma, M. J., Burd, H., Bhattacharyya, A., Rhodes, L. D., Kaul, R., Strom, M. S. (2008). Genome Sequence of the Fish Pathogen Renibacterium salmoninarum Suggests Reductive Evolution away from an Environmental Arthrobacter Ancestor. J. Bacteriol. 190: 6970-6982 [Abstract] [Full Text]  
  • Wiens, G. D., Owen, J. (2005). Mapping of Neutralizing Epitopes on Renibacterium salmoninarum p57 by Use of Transposon Mutagenesis and Synthetic Peptides. Appl. Environ. Microbiol. 71: 2894-2901 [Abstract] [Full Text]  
  • Rhodes, L. D., Coady, A. M., Deinhard, R. K. (2004). Identification of a Third msa Gene in Renibacterium salmoninarum and the Associated Virulence Phenotype. Appl. Environ. Microbiol. 70: 6488-6494 [Abstract] [Full Text]  


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