Ornithobacterium rhinotracheale has neuraminidase activity causing desialylation of chicken and turkey serum and tracheal mucus glycoproteins

Saša Kastelic, Rebeka Lucijana Berčič, Ivanka Cizelj, Mateja Benčina, Laszlo Makrai, Olga Zorman-Rojs, Mojca Narat, Magne Bisgaard, Henrik Christensen, Dušan Benčina

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Neuraminidases (sialidases) are virulence factors of several poultry pathogens. Ornithobacterium rhinotracheale is a well known poultry pathogen causing respiratory disease in chickens and turkeys all over the world. We investigated whether O. rhinotracheale has neuraminidase enzymatic activity (NEAC). We tested NEAC in 47 O. rhinotracheale strains isolated from turkeys and chickens in eight countries. All strains showed relatively strong NEAC and considerable levels of NEAC were detected also in " cell-free supernatants" of their pelleted cells. Zymography using neuraminidase-specific chromogenic substrate indicated that a protein with molecular mass of ∼40kDa and isoelectric point (pI) of ∼8.0 is a putative neuraminidase of O. rhinotracheale. Notably, the genome of the type strain of O. rhinotracheale, DSM 15997 contains a gene (Ornrh_1957) encoding a putative neuraminidase with such Mw (39.5kDa) and pI (8.5). We sequenced a corresponding genomic region of 20 O. rhinotracheale strains and found five distinct types of the neuraminidase gene (termed nanO) sequences. Most diversified nanO sequence was found in two strains isolated from chickens in Hungary in 1995. Their nanO sequences differ from that of the type strain (LMG 9086T) in 27 nucleotides. O. rhinotracheale neuraminidase showed capacity to cleave sialic acid from chicken and turkey glycoproteins. It cleaved sialic acid from SAα(2-6)gal moiety of their serum proteins, including immunoglobulin G (IgG) and transferrin. O. rhinotracheale also desialylated chicken and turkey tracheal mucus glycoprotens with SAα(2-3)gal moieties. This study provides the first evidence that O. rhinotracheale has neuraminidase which can desialylate glycoproteins of its natural hosts.

Original languageEnglish
Pages (from-to)707-712
Number of pages6
JournalVeterinary Microbiology
Volume162
Issue number2-4
DOIs
Publication statusPublished - Mar 23 2013

Keywords

  • Desialylation
  • Neuraminidase activity
  • Ornithobacterium rhinotracheale
  • Poultry glycoproteins

ASJC Scopus subject areas

  • Microbiology
  • veterinary(all)

Fingerprint Dive into the research topics of 'Ornithobacterium rhinotracheale has neuraminidase activity causing desialylation of chicken and turkey serum and tracheal mucus glycoproteins'. Together they form a unique fingerprint.

  • Cite this

    Kastelic, S., Berčič, R. L., Cizelj, I., Benčina, M., Makrai, L., Zorman-Rojs, O., Narat, M., Bisgaard, M., Christensen, H., & Benčina, D. (2013). Ornithobacterium rhinotracheale has neuraminidase activity causing desialylation of chicken and turkey serum and tracheal mucus glycoproteins. Veterinary Microbiology, 162(2-4), 707-712. https://doi.org/10.1016/j.vetmic.2012.09.018