Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 154 (2008), 207-216; DOI  10.1099/mic.0.2007/011528-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kim, H. G.
Right arrow Articles by Park, Y. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, H. G.
Right arrow Articles by Park, Y. K.
Agricola
Right arrow Articles by Kim, H. G.
Right arrow Articles by Park, Y. K.
Microbiology 154 (2008), 207-216; DOI  10.1099/mic.0.2007/011528-0
© 2008 Society for General Microbiology

N-terminal residues of SipB are required for its surface localization on Salmonella enterica serovar Typhimurium

Hyeon Guk Kim1,{dagger}, Bae Hoon Kim1,2,{dagger}, Jin Seok Kim1, Jeong Seon Eom1, Iel-Soo Bang3, Seong Ho Bang4, In Soo Lee5 and Yong Keun Park1

1 Laboratory of Microbial Genetics, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea
2 Institute of Biotechnology, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea
3 Department of Microbiology and Immunology, Chosun University School of Dentistry, Gwang ju 501-759, Republic of Korea
4 Department of Biological Science, Hanseo University, Seosan 356-706, Republic of Korea
5 Department of Microbiology, Hannam University, DaeJeon 300-791, Republic of Korea

Correspondence
Yong Keun Park
ykpark{at}korea.ac.kr

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.

Abbreviations: DOC, sodium deoxycholate; IFA, immunofluorescence assay; SPI-1, Salmonella pathogenicity island 1; T3SS, type III secretion system

{dagger}These authors contributed equally to this work.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2008 Society for General Microbiology.