Your browser doesn't support javascript.
loading
Characterization of a novel Type-I Crustin (carcininPm2) from black tiger shrimp Penaeus monodon.
Donpudsa, Suchao; Piaprad, Orawan; Tassanakajon, Anchalee; Rimphanitchayakit, Vichien; Visetnan, Suwattana.
Afiliação
  • Donpudsa S; Department of Chemistry, Faculty of Science, Srinakharinwirot University, Bangkok, 10110, Thailand.
  • Piaprad O; Department of Chemistry, Faculty of Science, Srinakharinwirot University, Bangkok, 10110, Thailand.
  • Tassanakajon A; Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Phyathai Road, Bangkok, 10330, Thailand.
  • Rimphanitchayakit V; Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Phyathai Road, Bangkok, 10330, Thailand.
  • Visetnan S; Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Phyathai Road, Bangkok, 10330, Thailand; Faculty of Dentistry, Bangkokthonburi University, Bangkok, 10170, Thailand. Electronic address: visetnan.s@gmail.com.
Fish Shellfish Immunol ; 148: 109520, 2024 May.
Article em En | MEDLINE | ID: mdl-38513915
ABSTRACT
Carcinins are type-I crustins from crustaceans and play an important role in innate immune system. In this study, type-I crustins, carcininPm1 and carcininPm2, from the hemocytes of Penaeus monodon were identified. Comparison of their amino acid sequences and the phylogenetic tree revealed that they were closely related to the other crustacean carcinin proteins, but were clustered into different groups of the carcinin proteins. The full-length amino acids of carcininPm1 and carcininPm2 were 92 and 111 residues, respectively. CarcininPm1 and carcininPm2 were expressed mainly in hemocytes and intestine compared to the other tissues. The expression of carcininPm1 and carcininPm2 were dramatically increased in early time of bacterial challenged shrimp hemocytes. In contrast, the carcininPm1 and carcininPm2 were expressed in response to late state of YHV-infected shrimp hemocytes where the copy number of virus was high. The recombinant carcininPm2 (rcarcininPm2) but not its WAP domain (rcarcininPm2_WAP) exhibited antimicrobial activity against Vibrio harveyi and Vibrio parahaemolyticus AHPND but not other bacteria tested. The rcarcininPm2 was able to prolong the survival rate of VH-treated post larval shrimp from about 102 h to 156 h. These studies indicated that the carcininPm2 possessed the potential and challenges as antibacterial in innate immunity of shrimp.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vibrio parahaemolyticus / Peptídeos Catiônicos Antimicrobianos / Penaeidae Limite: Animals Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vibrio parahaemolyticus / Peptídeos Catiônicos Antimicrobianos / Penaeidae Limite: Animals Idioma: En Ano de publicação: 2024 Tipo de documento: Article