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Infection and Immunity, January 2006, p. 183-191, Vol. 74, No. 1
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.1.183-191.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Role in Virulence of a Brucella abortus Protein Exhibiting Lectin-Like Activity

Tracy H. Vemulapalli,1,{dagger} Ramesh Vemulapalli,2 Gerhardt G. Schurig,1 Stephen M. Boyle,1 and Nammalwar Sriranganathan1*

Center for Molecular Medicine and Infectious Diseases, Department of Biomedical Sciences and Pathobiology, VA-MD Regional College of Veterinary Medicine, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061,1 Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, Indiana 479072

Received 11 July 2005/ Returned for modification 12 August 2005/ Accepted 26 September 2005

Brucella abortus is a facultative, intracellular zoonotic pathogen which can cause undulant fever in humans and abortions in cattle. A 14-kDa protein of B. abortus was previously identified to be immunogenic in animals infected with Brucella spp. In this study, we discovered that the 14-kDa protein possessed immunoglobulin binding and hemagglutination properties that appeared to be based on the protein's lectin-like properties. Hemagglutination inhibition experiments suggested that the 14-kDa protein has affinity towards mannose. Disruption of the gene encoding the 14-kDa protein in virulent B. abortus strain 2308 induced a rough-like phenotype with an altered smooth lipopolysaccharide (LPS) immunoblot profile and a significant reduction in the bacterium's ability to replicate in mouse spleens. However, the mutant strain was stably maintained in mouse spleens at 2.0 to 2.6 log10 CFU/spleen from day 1 to week 6 after intraperitoneal inoculation with 4.65 log10 CFU. In contrast to the case for the smooth virulent strain 2308, in the rough attenuated strain RB51 disruption of the 14-kDa protein's gene had no effect on the mouse clearance pattern. These findings indicate that the 14-kDa protein of B. abortus possesses lectin-like properties and is essential for the virulence of the species, probably because of its direct or indirect role in the synthesis of smooth LPS.

* Corresponding author. Mailing address: Center for Molecular Medicine and Infectious Diseases, 1410 Prices Fork Rd., Blacksburg, VA 24061. Phone: (540) 231-7171. Fax: (540) 231-3426. E-mail: nathans{at}vt.edu.

Editor: W. A. Petri, Jr.

{dagger} Present address: Laboratory Animal Medicine Residency Program, Department of Veterinary Pathobiology, Purdue University, West Lafayette, Ind.

Infection and Immunity, January 2006, p. 183-191, Vol. 74, No. 1
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.1.183-191.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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