Abstract:
:The Cj1169c-encoded putative protein of Campylobacter was expressed and purified from E. coli after sequence optimization. The purified protein allowed the production of a specific rabbit antiserum that was used to study the protein expression in vitro and its subcellular localization in the bacterial cell and putative interactions with other proteins. This protein is produced in Campylobacter and it clearly localizes into the periplasmic space. The level of protein production depends on factors, including pH, temperature, osmolarity, and growth phase suggesting a role in the Campylobacter environmental adaptation. The cysteine residues present in the sequence are probably involved in disulfide bridges, which may promote covalent interactions with other proteins of the Campylobacter envelope.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Aliouane S,Pagès JM,Bolla JMdoi
10.1007/s00284-015-0980-xsubject
Has Abstractpub_date
2016-05-01 00:00:00pages
511-7issue
5eissn
0343-8651issn
1432-0991pii
10.1007/s00284-015-0980-xjournal_volume
72pub_type
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