Beta-keratin 75-80% of the amino acids in silk, another 10-15% is serine and the final 10% contain bulky side chains such as in tyr, arg, val, asp, and glu. Beta-keratin β-keratin or beta-keratin is a member of a structural protein family found in the epidermis of reptiles and birds . β-keratins were named so because they are components of epidermal stratum corneum rich in stacked β pleated sheets, in contrast to alpha-keratins, intermediate-filament proteins also found in stratum corneum and rich in alpha helices. Because the accurate use of the term "keratin" is limited to the alpha-keratins, the term "beta-keratins" in
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