Applied and Environmental Microbiology, February 2008, p. 907-911, Vol. 74, No. 3
0099-2240/08/$08.00+0 doi:10.1128/AEM.02052-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Isolation and Characterization of Vibrio tubiashii Outer Membrane Proteins and Determination of a toxR Homolog
,
J. Jean-Gilles Beaubrun,1,2*
M. H. Kothary,2
S. K. Curtis,2
N. C. Flores,2
B. E. Eribo,1 and
B. D. Tall2
Howard University, Washington, D.C. 20050,1
U.S. Food and Drug Administration, Laurel, Maryland 207082
Received 7 September 2007/
Accepted 30 November 2007
Outer membrane proteins (OMPs) expressed by Vibrio tubiashii under different environmental growth conditions were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and PCR analyses. Results showed the presence of a 38- to 40-kDa OmpU-like protein and ompU gene, a maltoporin-like protein, several novel OMPs, and a regulatory toxR homolog.
* Corresponding author. Mailing address: Office no. 3655, White Oak Building 21 (HFD-003), Office of Pharmaceutical Science, Center for Drug Evaluation and Research, U.S. Food and Drug Administration, 10903 New Hampshire Ave., Silver Spring, MD 20993. Phone: (301) 796-1501. Fax: (301) 796-9732. E-mail: junia.beaubrun{at}fda.hhs.gov
Published ahead of print on 14 December 2007.
Supplemental material for this article may be found at http://aem.asm.org/.
Applied and Environmental Microbiology, February 2008, p. 907-911, Vol. 74, No. 3
0099-2240/08/$08.00+0 doi:10.1128/AEM.02052-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Copyright © 2008 by the American Society for Microbiology. All rights reserved.