N-glycans from porcine trachea and lung: predominant NeuAcα2-6Gal could be a selective pressure for influenza variants in favor of human-type receptor

PLoS One. 2011 Feb 9;6(2):e16302. doi: 10.1371/journal.pone.0016302.

Abstract

It is known that pigs acted as "mixing vessels" for genesis of a new reassortant influenza strain responsible for pandemic H1N1 2009. However, the host factors driving the evolution of a reassorted virus in pigs to 'jump species' resulting in a human outbreak remain unclear. N-glycans derived from the porcine respiratory tract were enzymatically released, fluorescent labeled with 2-aminopyridine, separated according to charge, size and hydrophobicity, and structurally identified by a two-dimensional (size and hydrophobicity) HPLC mapping technique and MALDI-TOF mass spectrometry before and after exo-glycosidase digestion. We found a 3-, 5-, and 13-fold increases in NeuAcα2-6, a preferable human influenza receptor, over NeuAcα2-3, an avian influenza receptor, from upper and lower parts of the porcine trachea towards the porcine lung, a major target organ for swine virus replication. The large proportion of NeuAcα2-6 may exert selective pressure for selection of influenza variants with altered receptor preference for this human-type α2-6 receptor, a crucial first step for generating a human pandemic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrate Sequence
  • Evolution, Molecular
  • Female
  • Humans
  • Lung / metabolism*
  • Lung / virology
  • Molecular Sequence Data
  • Orthomyxoviridae / genetics*
  • Orthomyxoviridae / metabolism
  • Orthomyxoviridae / physiology
  • Polysaccharides / chemistry
  • Polysaccharides / isolation & purification
  • Polysaccharides / metabolism*
  • Receptors, Cell Surface / metabolism*
  • Selection, Genetic*
  • Sialyltransferases / metabolism
  • Substrate Specificity
  • Swine*
  • Trachea / metabolism*
  • Trachea / virology
  • Virus Replication

Substances

  • Polysaccharides
  • Receptors, Cell Surface
  • Sialyltransferases