Abstract
The recognition and inactivation of toxins and pathogens are mediated by a combination of cell-free and cellular mechanisms. A number of soluble and membrane-bound pattern recognition molecules interact with elicitors to become involved in both cell-free inactivation as well as cellular uptake reactions. Here we describe the possible recognition and effector function of key arthropod immune proteins, such as peroxinectin, hemolin, and hemomucin, as an outcome of changes in adhesiveness, which drive self-assembly reactions leading to cell-free coagulation and cellular uptake reactions. The fact that some of these proteins are essential for immune and developmental functions in some species, but are not found in closely related species, may point to the existence of multiprotein assemblies, which are conserved at the mechanistic level and can function with more than one combination of protein constituents.
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