Colicin Z, a structurally and functionally novel colicin type that selectively kills enteroinvasive Escherichia coli and Shigella strains

Logo poskytovatele
Logo poskytovatele
Logo poskytovatele

Varování

Publikace nespadá pod Filozofickou fakultu, ale pod Lékařskou fakultu. Oficiální stránka publikace je na webu muni.cz.
Autoři

MICENKOVÁ Lenka BOSÁK Juraj KUČERA Jiří HRALA Matěj DOLEJSOVA Tereza ŠEDO Ondrej LINKE Dirk FISER Radovan ŠMAJS David

Rok publikování 2019
Druh Článek v odborném periodiku
Časopis / Zdroj Scientific reports
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
www https://www.nature.com/articles/s41598-019-47488-8.pdf
Doi http://dx.doi.org/10.1038/s41598-019-47488-8
Klíčová slova NUCLEOTIDE-SEQUENCE; BACTERIAL; IMMUNITY; DOMAIN; GENES; ORGANIZATION; PYOCINS; IMPORT; DNA
Popis Colicin production in Escherichia coli (E. coli) strains represents an important trait with regard to microbial survival and competition in the complex intestinal environment. A novel colicin type, colicin Z (26.3 kDa), was described as a product of an original producer, extraintestinal E. coli B1356 strain, isolated from the anorectal abscess of a 17 years-old man. The 4,007 bp plasmid (pColZ) was completely sequenced and colicin Z activity (cza) and colicin Z immunity (czi) genes were identified. The cza and czi genes are transcribed in opposite directions and encode for 237 and 151 amino acid-long proteins, respectively. Colicin Z shows a narrow inhibitory spectrum, being active only against enteroinvasive E. coli (EIEC) and Shigella strains via CjrC receptor recognition and CjrB- and ExbB-, ExbD-mediated colicin translocation. All tested EIEC and Shigella strains isolated between the years 1958-2010 were sensitive to colicin Z. The lethal effect of colicin Z was found to be directed against cell wall peptidoglycan (PG) resulting in PG degradation, as revealed by experiments with Remazol Brilliant Blue-stained purified peptidoglycans and with MALDI-TOF MS analyses of treated PG. Colicin Z represents a new class of colicins that is structurally and functionally distinct from previously studied colicin types.
Související projekty:

Používáte starou verzi internetového prohlížeče. Doporučujeme aktualizovat Váš prohlížeč na nejnovější verzi.