CHARACTERIZATION OF A NATURAL HEMAGGLUTININ WITH AFFINITY FOR ACETYLATED AMINOSUGARS IN THE SERUM OF THE MARINE PRAWN, PENAEUS-INDICUS (EDWARDS,H.MILNE)
R. Maheswari et al., CHARACTERIZATION OF A NATURAL HEMAGGLUTININ WITH AFFINITY FOR ACETYLATED AMINOSUGARS IN THE SERUM OF THE MARINE PRAWN, PENAEUS-INDICUS (EDWARDS,H.MILNE), Fish & shellfish immunology, 7(1), 1997, pp. 17-28
A natural haemagglutinin was detected in the serum of the marine prawn
Penaeus indicus, using mammalian erythrocytes (RBC). The haemagglutin
ation profile and cross-adsorption tests revealed a strong reactivity
with human A RBC, and trypsinisation of this RBC type enhanced their s
usceptibility for agglutination by the serum. The agglutinating activi
ty did not require Ca2+ or Mg2+, was insensitive to EDTA and EGTA, sta
ble in a wide pH range (pH 3 to 9) and labile at or above 80 degrees C
. Ammonium sulphate and trichloroacetic acid completely precipitated t
he haemagglutinating activity from serum, suggesting it is a protein o
r glycoprotein. However, neither trypsin treatment nor periodate oxida
tion of serum abrogated the agglutinating activity. Haemagglutination-
inhibition assays performed with several carbohydrates and glycoprotei
ns revealed a unique specificity of serum agglutinin for acetylated am
inosugars and that the presence of the acetyl group was essential for
agglutinin-ligand interaction. The haemagglutinating activity of the s
erum could be specifically inhibited by lipopolysaccharide from Salmon
ella abortus equi, but not with lipopolysaccharide from five other bac
terial species. (C) 1997 Academic Press Limited.