Brugia malayi: patterns of expression of surface-associated antigens

Exp Parasitol. 1992 Feb;74(1):57-68. doi: 10.1016/0014-4894(92)90139-2.

Abstract

Patterns of expression of surface-associated antigens were analyzed in the filarial nematode Brugia malayi immediately prior, and during development in the vertebrate host. Two surface-associated protein molecules, i.e., accessible to surface radioiodination and soluble in aqueous buffers, were investigated: Mrs 29-30,000 and 16,000, both of which are antigenic in infected animals. The Mr 29-30,000 glycoprotein is expressed in a surface-associated manner by adult worms and by fourth-stage larvae, but is not detectable in preparasitic third-stage larvae. The 16,000 component, which appears not to be glycosylated, is surface-associated in adult worms and fourth-stage larvae. In contrast to the 29-30,000 glycoprotein, the 16,000 protein is also expressed both by pre- and postparastic third-stage larvae. However, it becomes surface-associated only after infection. Thus, immediately prior, and during development within the vertebrate host, B. malayi displays at least two different patterns of expression of surface-associated antigens: (i) de novo, intiated either immediately after infection (phase specific) or during genesis of the fourth-stage larva (stage specific); (ii) continuous, but with phase-dependent surface exposure of previously cryptic antigens, during the transition from intermediate to definitive host.

MeSH terms

  • Animals
  • Antigens, Helminth / biosynthesis*
  • Antigens, Surface / biosynthesis*
  • Brugia / growth & development
  • Brugia / immunology*
  • Electrophoresis, Polyacrylamide Gel
  • Elephantiasis, Filarial / parasitology
  • Gerbillinae
  • Glycoproteins / biosynthesis
  • Helminth Proteins / biosynthesis
  • Larva / immunology
  • Male
  • Molecular Weight
  • Precipitin Tests

Substances

  • Antigens, Helminth
  • Antigens, Surface
  • Glycoproteins
  • Helminth Proteins