HEBP1 |
hEBSA |
CKLFSF3 |
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Hebraein is an 11 kDa antimicrobial peptide with a unique amino acid sequence, purified from the hemolymph of fed female Amblyomma hebraeum ticks. The cDNA encodes a protein of 102 amino acids with no significant similarity to any known protein. The protein contains 6 cysteine residues and has 9 histidine residues in its C-terminal domain that are mainly present as HX repeats. The secondary structure prediction is very clearly all alpha-helical (4-6 helices) except for a very short extension at the C terminus. Recombinant native hebraein shows strong antimicrobial activities, which is reduced in histidine-deficient mutants. The expression of hebraein is up-regulated by blood feeding and the protein may play a role in innate immune defense.
For other proteins/peptides with functions in innate immunity and/or antimicrobial activities see also:
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