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Proteolytic cleavage of the Chlamydia pneumoniae major outer membrane protein in the absence of Pmp10
Author(s) -
Juul Nicolai,
Timmerman Evy,
Gevaert Kris,
Christiansen Gunna,
Birkelund Svend
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700447
Subject(s) - bacterial outer membrane , biology , proteome , cleavage (geology) , gene , membrane protein , chlamydophila pneumoniae , microbiology and biotechnology , chlamydiaceae , chlamydiales , genome , virulence , bacteria , escherichia coli , biochemistry , genetics , membrane , paleontology , fracture (geology)
The genome of the obligate intracellular bacteria Chlamydia pneumoniae contains 21 genes encoding polymorphic membrane proteins (Pmp). While no function has yet been attributed to the Pmps, they may be involved in an antigenic variation of the Chlamydia surface. It has previously been demonstrated that Pmp10 is differentially expressed in the C. pneumoniae CWL029 isolate. To evaluate whether the absence of Pmp10 in the outer membrane causes further changes to the C. pneumoniae protein profile, we subcloned the CWL029 isolate and selected a clone with minimal Pmp10 expression. Subsequently, we compared the proteome of the CWL029 isolate with the proteome of the subcloned strain and identified a specific cleavage of the C‐terminal part of the major outer membrane protein (MOMP), which occurred only in the absence of Pmp10. In contrast, when Pmp10 was expressed we predominantly observed full‐length MOMP. No other proteins appeared to be regulated according to the presence or absence of Pmp10. These results suggest a close association between MOMP and Pmp10, where Pmp10 may protect the C‐terminal part of MOMP from proteolytic cleavage.