Epidermin

The posttranslationally modified cross-link S -[(Z)-2-aminovinyl]-D-cysteine (AviCys Figure 1) has been found at the C-terminus of the lantibiotics epidermin, gallidermin, cypemycin, and mutacin III. A group of decarboxylases, called LanD proteins, are encoded in the lantibiotic gene clusters and are responsible for this modification. The first LanD protein characterized was EpiD from the epidermin-producing strain S. epidermis EpiA and EpiD were separately overexpressed in E. coliand purified. 

Section 5.08.4). Engineered expression systems have also been established for subtilin/ Pep5/" ° epidermin and gallidermin/ mutacin lacticin 3147 436,142 mersacidin. " " In these studies, the immunity genes were typically also required for generating successful expression systems. 

With respect to synthetic methods, the most thoroughly investigated lanthionine from the group of alkylated lanthionines is threo-3-methyllanthionine (2), a lanthionine which is also found in a number of natural peptides such as nisin[12l and epidermin.14 In this section, some of the synthetic methods are compared and discussed with respect to their relative applicability and their possible extension to other alkylated lanthionines. 

Fibrinogen is a fibrous protein that was first classified with keratin, myosin, and epidermin based on its 5.1 A repeat in wide-angle X-ray diffraction patterns (Bailey et al., 1943), which was later discovered to be associated with the Q-helical coiled-coil structure. It is a glycoprotein normally present in human blood plasma at a concentration of about 2.5 g/L and is essential for hemostasis, wound healing, inflammation, angiogenesis, and other biological functions. It is a soluble macromolecule, but forms a clot or insoluble gel on conversion to fibrin by the action of the... 

Another common posttranslational modification found in mature lantibiotics is a C-terminal AviCys (Fig. la). This residue is formed by EpiD in epidermin (18). Currently, not much is known about the enzymes that catalyze formation of other unique lantibiotic residues. The cinnamycin gene cluster was cloned recently (19), which set the stage for studies to determine which gene products are responsible for lysinoalanine and fi-hydroxy aspartate formation. 

Hu T, Khambatta ZS, Hayden PJ, Bolmarcich J, Binder RL, Robinson MK, Carr GJ, Tiesman JP, Jarrold BB, Osborne R, Reichling TD, Nemeth ST, Aardema MJ (2010) Xenobiotic metabolism gene expression in the EpiDermin vitro 3D human epidermis model compared to human skin. Toxicol In Vitro 24 1450-1463. doi 10.1016/j.tiv.2010.03.013... 

H. G. (1998) Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30, 317-327. 

Epidermin. [Henkel/Cospha] Polyvalent tissue complexes i o. for ag g and sensitive sl. ... 

Epidermin. enkel/Coqtha] Polyvalent tissue conqrlexes prods, for ag and sonsitive sidn. 

No studies of amino acids have been made on these proteins as yet that is best left until we are more certain about the purity of the fractions, There is no suggestion that the proteins contain any nucleic acid as the phosphorus content is nil except in one case (inner level, non-fibrous protein of Table II). But a number of determinations of sulfur content have been made, and these are of obvious interest. Of the two main fractions, that precipitating at pH 5.5 is referred to as the fibrous protein or epidermin, and that precipitating at pH 4.5 as the nonfibrous protein. 

Fig. 5. X-ray fiber photograph of epidermal protein (epidermin), a-form.

---