M. Robinson et al., NONSPECIFIC-BINDING OF MOUSE IGG1 TO HELIGMOSOMOIDES-POLYGYRUS - PARASITE HOMOGENATE CAN AFFINITY PURIFY MOUSE MONOCLONAL-ANTIBODIES, Parasitology, 114, 1997, pp. 79-84
A characteristic feature of infections with the nematode parasite of m
ice Heligmosomoides polygyrus, is a marked IgG1 hypergammaglobulinaemi
a. A possible source for this immunoglobulin has recently been demonst
rated, through evidence that H. polygyrus adult worm homogenate (AWH)
can induce the in vitro production of non-specific IgG1 from mouse lym
phocytes. To determine the interactions between this immunoglobulin an
d the parasite, the ability of IgG1 to bind to AWH of H. polygyrus was
investigated. Protein (Western) blotting indicated that mouse monoclo
nal antibodies are able to bind non-specifically to selected parasite
antigens. Furthermore, by binding H. polygyrus adult worm homogenate t
o cyanogen bromide (CNBr)-activated Sepharose CL-4B, an affinity colum
n was prepared which could be used to efficiently purify mouse IgG1 mo
noclonal antibodies. These antibodies were eluted from the affinity co
lumn and still retained their original specificity. These results indi
cate that H. polygyrus not only induces the production of non-specific
IgG1 by the host, it can also bind this immunoglobulin to its own spe
cific proteins. Thus, it is possible that IgG1 produced during a prima
ry infection with H. polygyrus may not entirely benefit the host.