Binding and degradation of lectins by components of rumen liquor

The binding of 15 different plant lectins to feed particles and microbes in rumen liquor, and their degradation were studied in vitro. The rate of degradation assessed from the label released when radioactive iodine-labelled lectins were incubated with rumen liquor conflicted with the rates calculated from measurements of the survival of the antigenic structure (immuno-rocket electrophoresis) or the biological function (haemagglutination) of the lectins. Thus solubilization of the radioactive label indicated that Concanavalin A (Con A), but not the soyabean agglutinin, SBA, or kidney bean phytohaemagglutinin, PHA-E3L, was stable to rumen proteolysis. In contrast, both SBA and PHA-E3L were shown by immuno-rocket electrophoresis or haemagglutination tests to be highly resistant to breakdown, while the degradation of Con A proceeded at a constant slow rate under the same conditions. This was in accord with the previously established general stability of lectins in the gut of single-stomach animals. Of the 15 lectins, SBA, favin (Vicia faba lectin) and Con A were bound by hay and the particle fraction of rumen liquor. This was, in part, specific and reversible in the presence of appropriate sugars. Most pure bacterial strains preferentially bound lectins with specificity for glucose/mannose (favin and Con A), while rumen fungi reacted with SBA. The level of binding was low with other lectins. However, inter-strain differences of lectin-binding were found in Selenomonas ruminantium and Ruminococcus flavefaciens. Clearly, as some lectins were not fully degraded in the rumen, they could be expected to depress the utilization of the diet not only in single-stomach animals but, possibly, also in ruminants.