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Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Research output: Contribution to journalReview article

Author(s)

Valerie J. Smith, J M O Fernandes, Graham D. Kemp, Chris Hauton

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Abstract

Crustins are antibacterial proteins of ca. 7-14 kDa with a characteristic four-disulphide core-containing whey acidic protein (WAP) domain, expressed by the circulating haemocytes of crustaceans. Over 50 crustin sequences have been now reported from a variety of decapods, including crabs, lobsters, shrimp and crayfish. Three main types seem to occur but all possess a signal sequence at the amino terminus and a WAP domain at the carboxyl end. Differences between types lie in the structure of the central region. Those crustins purified as the native protein or expressed recombinantly all kill Gram-positive bacteria, and gene studies have shown that they are constitutively expressed, often at high levels, but show no consistent patterns of change in expression following injection of bacteria. This variable response to infection is enigmatic but indicates that these proteins could perform additional functions, perhaps as immune regulators in recovery from wounding, trauma or physiological stress. (c) 2008 Elsevier Ltd. All rights reserved.

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Original languageEnglish
Pages (from-to)758-772
Number of pages15
JournalDevelopmental and Comparative Immunology
Volume32
DOIs
StatePublished - 2008

    Research areas

  • antibacterial peptides, crustins, whey acidic protein domain, four-disulphide core, innate defence effectors, invertebrate immunity, defensins, SHRIMP PENAEUS-MONODON, LITOPENAEUS-VANNAMEI HEMOCYTES, LOBSTER HOMARUS-AMERICANUS, CHITIN-BINDING ACTIVITY, PACIFIC WHITE SHRIMP, ANTIMICROBIAL PEPTIDES, TIGER SHRIMP, RECOMBINANT EXPRESSION, CARCINUS-MAENAS, GENE-EXPRESSION

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