N-terminal residues of SipB are required for its surface localization on Salmonella enterica serovar Typhimurium
- Authors
- Kim, Hyeon Guk; Kim, Bae Hoon; Kim, Jin Seok; Eom, Jeong Seon; Bang, Lel-Soo; Bang, Seong Ho; Lee, In Soo; Park, Yong Keun
- Issue Date
- Jan-2008
- Publisher
- MICROBIOLOGY SOC
- Citation
- MICROBIOLOGY-SGM, v.154, pp.207 - 216
- Indexed
- SCIE
SCOPUS
- Journal Title
- MICROBIOLOGY-SGM
- Volume
- 154
- Start Page
- 207
- End Page
- 216
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/124459
- DOI
- 10.1099/mic.0.2007/011528-0
- ISSN
- 1350-0872
- Abstract
- SipB, one of the invasion proteins encoded in Salmonella pathogenicity island 1 (SPI-1), is known to be secreted outside the cell, where it functions as a translocon by assembling into a host-cell plasma membrane-integral structure. Here, we confirmed that wild-type SipB could be localized to the bacterial outer membrane, and further showed that its localization was dependent on extracellular secretion, and was independent of the presence of the SipD protein. Proteinase K susceptibility and immunofluorescence assays indicated that SipB was not incorporated into the outer membrane, but rather was displayed on the bacterial surface. Finally, mutation studies revealed that the N-terminal 100-140 aa (especially amino acids 135-138) of SipB were required for its localization on the bacterial outer membrane.
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Collections - College of Life Sciences and Biotechnology > Division of Life Sciences > 1. Journal Articles
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