NONSPECIFIC-BINDING OF MOUSE IGG1 TO HELIGMOSOMOIDES-POLYGYRUS - PARASITE HOMOGENATE CAN AFFINITY PURIFY MOUSE MONOCLONAL-ANTIBODIES

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.