Mechanism study on a new antimicrobial peptide Sphistin derived from the N-terminus of crab histone H2A identified in haemolymphs of Scylla paramamosain

Fish and Shellfish Immunology

Volumn 47, Issue 2, 2015, Pages 833-846

  Chen, Bei ^a   Fan, Dan Qing ^a   Zhu, Ke Xin ^a   Shan, Zhong Guo ^a   Chen, Fang Yi ^a   Hou, Lin ^a   Cai, Ling ^a   Wang, Ke Jian ^a  

^a XIAMEN UNIVERSITY   (China)

Author keywords

Antimicrobial activity; Antimicrobial mechanism; Cytotoxicity; Histone; Scylla paramamosain; Sphistin

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; ARTHROPOD PROTEIN; COMPLEMENTARY DNA; HISTONE; MESSENGER RNA;

AMINO ACID SEQUENCE; ANIMAL; ANTIBODY SPECIFICITY; BACTERIUM; BRACHYURA; CHEMISTRY; DRUG EFFECTS; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYLOGENY; PHYSIOLOGY; SEQUENCE ALIGNMENT; VIROLOGY; WHITE SPOT SYNDROME VIRUS; YEAST;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; ARTHROPOD PROTEINS; BACTERIA; BASE SEQUENCE; BRACHYURA; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GENE EXPRESSION REGULATION; HISTONES; MOLECULAR SEQUENCE DATA; ORGAN SPECIFICITY; PHYLOGENY; RNA, MESSENGER; SEQUENCE ALIGNMENT; WHITE SPOT SYNDROME VIRUS 1; YEASTS;

EID: 84945543105     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2015.10.010     Document Type: Article

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