RRC ID 69897
Author Vo LK, Tran NT, Kubo Y, Sahashi D, Komatsu M, Shiozaki K.
Title Enhancement of Edwardsiella piscicida infection, biofilm formation, and motility caused by N-acetylneuraminate lyase.
Journal Glycoconj J
Abstract Sialic acid and its catabolism are involved in bacterial pathogenicity. N-acetylneuraminate lyase (NAL), which catalyzes the reversible aldol cleavage of sialic acid to form N-acetyl-D-mannosamine in the first step of sialic acid degradation, has been recently investigated to elucidate whether NAL enhances bacterial virulence; however, the role of NAL in bacterial pathogenicity remains unclear. In the present study, we demonstrated that the existence of two enzymes in Edwardsiella piscicida, referred to as dihydrodipicolinate synthase (DHDPS) and NAL, induced the cleavage/condensation activity toward sialic acids such as N-acetylneuraminic acid, N-glycolylneuraminic acid and 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonic acid. NAL enhanced cellular infection in vitro and suppressed the survival rate in zebrafish larvae in bath-infection in vivo, whereas DHDPS did not. Furthermore, NAL strongly activated the expression of E. piscicida phenotypes such as biofilm formation and motility, whereas DHDPS did not. Besides, the gene expression level of nanK, nanE, and glmU were up-regulated in the NAL-overexpressing strain, along with an increase in the total amount of N-acetylglucosamine.
Volume 39(3)
Pages 429-442
Published 2022-6-1
DOI 10.1007/s10719-022-10045-z
PII 10.1007/s10719-022-10045-z
PMID 35192095
MeSH Animals Bacterial Proteins / genetics Bacterial Proteins / metabolism Biofilms Edwardsiella N-Acetylneuraminic Acid* / metabolism Oxo-Acid-Lyases Zebrafish*
IF 2.197
Resource
Human and Animal Cells GAKS(RCB1452)