Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus

Christie, Andrew E.; Rus, Szymon; Goiney, Christopher C.; Smith, Christine M.; Towle, David W.; Dickinson, Patsy S.

doi:10.1016/j.molimm.2007.02.028

Cited by 34 publications

(14 citation statements)

References 33 publications

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“…4), while CAP-2 likely represented the predicted antimicrobial peptide for H. americanus, Hoa-crustin (Fig. 5) [10].…”

Section: Resultsmentioning

confidence: 99%

“…Initial lyophilisation and resuspension of the haemocyte lysate prior to extraction by reverse phase chromatography enhanced recovery of CAP-1 and CAP-2 (data not shown). CAP-1 was found to have similarities to temporins while CAP-2 was presumptively identified as the predicted H. americanus crustin-like peptide (Hoa-crustin) based on similarities in the amino acid sequences and molecular weights [10].…”

Section: Discussionmentioning

confidence: 99%

“…These include the tachyplesins and polyphemusins of the Chelicerata, penaeidins, crustins, and callinectin in the Crustacea, defensins and mytilins in Mollusca, and styelin and clavalin in tunicates. Recently, a crustin-like peptide, Hoa-crustin, was predicted for H. americanus using a multi-tissue EST library [10]. A sequence closely matching Hoa-crustin has also been identified and studied in the European lobster Homarus gammarus [11,12].…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus

Battison

Summerfield

Patrzykat

2008

Fish & Shellfish Immunology

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“…4), while CAP-2 likely represented the predicted antimicrobial peptide for H. americanus, Hoa-crustin (Fig. 5) [10].…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus

Battison

Summerfield

Patrzykat

2008

Fish & Shellfish Immunology

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“…These types of crustins are present mainly in crabs, lobsters and crayfish (the Pleocyemata) [11,32,[35][36][37] (Table 1). We designate them as Type I as they all show a similar domain arrangement as carcinin, the first crustacean WAP domain containing AMP to be found [9].…”

Section: Crustin Typesmentioning

confidence: 99%

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Smith

Fernandes²,

Kemp

et al. 2008

Developmental & Comparative Immunology

236

169

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Crustins are antibacterial proteins of ca 7-14 kDa with a characteristic four disulphide corecontaining 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.Prof Kenneth Soderhall Co-Editor in Chief Developmental and Comparative Immunology Dear Kenneth I attach the revised manuscript for the invited review, Crustins: enigmatic WAP domaincontaining antibacterial proteins from crustaceans, for which all the referees comments have been addressed. Below is a summary of changes made.1. Two of the reviewers have issues with the SS tree (formerly Fig 2), with reviewer 2 making the point that the functional WAP domain will more usefully indicate relationships rather than the SS. We do not concur with the comment that the signal sequence (SS) tree is unnecessary but do accept that its placement in the article could be better and that it could be more fully discussed. Importantly, the SS radiation tree did not drive the 3-type classification, rather it was led by the overall domain organisation of the various types that we judged, from our starting definition, to be within the crustin 'family'. The region of variation is mainly in the 'central' region of the molecule, ie between the SS and WAP domain. We constructed the SS and WAP domain trees to test if the suggested classification was supported, independently by phylogenies within these regions. We believe that they do and the inclusion of both trees, rather than just a tree for the WAP domain, makes the case for the classification of crustins into Types I, II or III, even stronger. We have therefore retained the SS radiation tree but discuss it more fully in the section on 'Relationships' (new pages 11 & 12) rather than its former position. We prefer not to add species identifiers to the as these will make it very 'busy' and untidy. We feel that Accession numbers are more appropriate than species names. Please note we have slightly modified the annotations by leaving ambiguous sequences out of the clusters marked by dotted or dashed lines.2. Referee 1 correctly points out that the argument (beginning in the last paragraph on pg 6 and continued on pg 7in the original m/s) that the signal sequence is probably not involved in crust...

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“…The classical example is SLPI that also contains double WAP domains and plays an important role in host defense and wound repair [9,10]. In recent years, several WAP-containing proteins have also been found in crustaceans including SWD from Litopenaeus vannamei [11], crustin-like from European lobster Homarus gammarus [12], crustin-like from the American lobster Homarus americanus [13], and carcinin from the shore crab Carcinus maenas [14]. However, all these proteins contain only a single WAP motif, the double WAP domain-containing proteins are rarely reported in invertebrates, except the one similar to mammalian SPLI and cloned from Litopenaeus vannamei recently [15].…”

Section: Introductionmentioning

confidence: 99%

Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus

Chen

He²,

Xu³

2008

Fish & Shellfish Immunology

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Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus

Cited by 34 publications

References 33 publications

Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus

Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus

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