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Comparative proteomic analysis of the outer membrane protein 43 (omp43) deficient Bartonella henselae
Jun-Gu Kang, Hee-Woo Lee, Sungjin Ko, Joon-Seok Chae*
Laboratory of Veterinary Internal Medicine, Research Institute and BK21 program for Veterinary science and College of Veterinary Medicine, Seoul National University, Seoul 08826, Korea
Correspondence to: Tel: +82-2-880-1279; Fax: +82-2-873-1213; E-mail: jschae@snu.ac.kr
Received: March 20, 2017; Revised: May 9, 2017; Accepted: June 8, 2017; Published online: July 10, 2017.
Outer membrane proteins (OMPs) of gram-negative bacteria constitute the first line of defense that protects the cells against environmental stresses including chemical, biophysical, and biological attacks. Although 43-kDa outer membrane protein (OMP43) is major porin protein among the Bartonella henselae-derived OMPs, its function remains unknown. In this study, OMP43-deficient mutant B. henselaeomp43) was generated to investigate function of OMP43. Interestingly, Δomp43 showed a weaker proliferative ability compared to wild type (WT) of B. henselae. To study the differences in proteomic expression between WT and Δomp43, two-dimensional gel electrophoresis-based proteomic analysis was performed. Based on COG functional assignment, we found 12 proteins to be associated with metabolism, 7 proteins associated with information storage and processing, and 3 proteins associated with cellular processing and signaling. By semi-quantitative RT-PCR, increase in tldD, efp, ntrX, pdhA, purB, and ATPA mRNA expression and decrease in Rho and yfeA mRNA expression was confirmed in Δomp43. In conclusion, this is the first report showing that loss of OMP43 expression in B. henselae leads to retarded proliferation. Furthermore, our proteomic data provide useful information for the further investigation of mechanism related to the growth of B. henselae.
Keywords: Bartonella, outer membrane protein, omp43, proliferation, proteomic

© 2017 The Korean Society of Veterinary Science.