Cs. Mcvay et al., PARTICIPATION OF PARASITE SURFACE GLYCOPROTEINS IN ANTIBODY-MEDIATED PROTECTION OF EPITHELIAL-CELLS AGAINST TRICHINELLA-SPIRALIS, Infection and immunity, 66(5), 1998, pp. 1941-1945
The L1 stage of the parasitic nematode Trichinella spiralis displays o
n its surface glycoproteins that are immunologically cross-reactive wi
th several larval excretory-secretory (ES) products, The basis for the
crossreactivity is tyvelose, the terminal residue on the complex glyc
ans shared by these surface and ES glycoproteins, In neonatal rats, ty
velose-specific monoclonal antibodies mediate the expulsion of larvae
from the intestine. The aim of the studies described in this report wa
s to determine holy antibody binding to larval surfaces contributes to
expulsion. In these experiments, which involve an in vitro assay of e
pithelial cell invasion, surface proteins on living larvae were biotin
ylated to distinguish them from ES products. Biotinylated and nonbioti
nylated larvae were cocultured with avidin, biotin-specific antibodies
, or anti-tyvelose monoclonal antibodies. Biotinylated larvae cultured
with avidin or biotin-specific antibodies invaded Madin-Darby canine
kidney (MDCK) cells equally as well as biotinylated larvae cultured wi
th medium alone. Anti-tyvelose monoclonal antibodies were highly prote
ctive in this assay; however, biotinylation of larval surfaces hindere
d the ability of anti-tyvelose monoclonal antibodies to prevent larval
invasion of epithelial cells. This correlated with a reduction in the
binding of anti-tyvelose antibody to biotinylated larval surfaces. Ou
r results indicate that antibody binding to surface glycoproteins cont
ributes to protection against T,spiralis invasion but that surface bin
ding alone is not sufficient for protection, Our findings support that
notion that protection is effected by cross-linking of ES products to
surface antigens.