GLIKOZYLACJA BIAŁEK MIKROORGANIZMÓW
RODZAJU CAMPYLOBACTER
Elżbieta Katarzyna Jagusztyn-Krynicka*, Joanna Życka
Karolina Tomczyk, Agnieszka Wyszyńska
Zakład Genetyki Bakterii, Instytut Mikrobiologii, Uniwersytet Warszawski
ul. Miecznikowa 1, 02-096 Warszawa, tel. 55 41 216, e-mail: kjkryn@biol.uw.edu.pl
Wpłynęło w maju 2005
l. Wstęp. 2. Ogólna charakterystyka procesów glikozylacji białek
Prokaryota. 3. Glikozylacja białek u Campylobacter. 3.1. O-glikozylacja białek u Campylobacter. 3.2. N-glikozylacja białek u
Campylobacter. 4. Podsumowanie
Protein glycosylation in Campylobacter
Abstract: Glycosylation is considered to be the most frequent system of protein modification in eukaryotic cells. It has been recently established that also many bacterial proteins are modified by glycosylation and now it is widely accepted that prokaryotes
(Archaea and Bacteria) express glycoproteins. In Gram-negative bacteria
0-linked as well as N-linked glycosylation has been reported. The first one was identified in many bacterial species whereas the
N-linked system seems to be rather restricted to e-Proteobacteria
(Campylobacter and Wolinella). In this review we provide a description of a mechanism of
Campylobacter protein glycosylation and a role of this process in bacterial pathogenesis. Sequencing of the
Campylobacter genomes evidently facilitates the analysis of posttranslational protein modification however many aspects of the process still remain to be determined.
1. Introduction. 2. General characterization of protein glycosylation in
Prokaryota. 3. Protein glycosylation in Campylobacter. 3.1.
O-glycosylation in Campylobacter. 3.2. N-glycosylation in
Campylobacter. 4. Summary
Słowa kluczowe: Campylobacter, glikozylacja
Key words: Campylobacter, glycosylation
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