Myosin to muscle cells (hence "myo-"(s) + "-in"), there is no single "myosin"; rather it is a very large superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous. The structure and function of myosin is globally conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba. Most myosin molecules are composed of a head, neck, and tail
Lectin MBL, the mannose-binding lectin, help mediate the first-line defense against invading microorganisms. Other lectins within the immune system are thought to play a role in self-nonself discrimination and they likely modulate inflammatory and autoreactive processes. Intelectins (X-type lectins) were shown to bind microbial glycans and may function in the innate immune system as well. Lectins may be involved in pattern recognition and pathogen elimination in the innate immunity of vertebrates including fishes. The function of lectins in plants (legume lectin) is still uncertain. Once thought to be necessary for rhizobia binding, this proposed function was ruled out through lectin-knockout transgene