Molecular cloning of crustins from the hemocytes of Brazilian penaeid shrimps

Rosa, Rafael Diego; Bandeira, Paula Terra; Barracco, Margherita Anna

doi:10.1111/j.1574-6968.2007.00866.x

Cited by 31 publications

(12 citation statements)

References 11 publications

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“…Numerous antimicrobial peptides, including many crustins, have been predicted utilising techniques such as EST libraries in recent years; however, the actual production and activity of these peptides is rarely confirmed [20,22,30]. Variance of CAP-2 from its anticipated activity (as representing Hoa-crustin) clearly illustrates the need to isolate, purify, and test these predicted peptides.…”

Section: Discussionmentioning

confidence: 97%

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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Section: Discussionmentioning

confidence: 97%

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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“…In the literature, this heterogeneous and complex crustin Type has been also subdivided into two sub-types, namely Type IIa or “Crustins”, most related to the first glycine-rich peptides identified in Litopenaeus species (Crustin Lv and Crustin Ls ) [ 4 ], and Type IIb or “Crustin-like”, homologues of the Cru Fc peptide from Fenneropenaeus chinensis [ 17 ] and the Crus-like Pm (or crustin Pm 7) peptide from P. monodon [ 18 ]. Interestingly, while Type IIa crustins have been identified in different penaeids [ 4 , 19 , 20 , 21 ], Type IIb crustins were only reported in Oriental (Asian) species [ 16 , 17 , 18 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Specific Molecular Signatures for Type II Crustins in Penaeid Shrimp Uncovered by the Identification of Crustin-Like Antimicrobial Peptides in Litopenaeus vannamei

et al. 2018

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Crustins form a large family of antimicrobial peptides (AMPs) in crustaceans composed of four sub-groups (Types I-IV). Type II crustins (Type IIa or “Crustins” and Type IIb or “Crustin-like”) possess a typical hydrophobic N-terminal region and are by far the most representative sub-group found in penaeid shrimp. To gain insight into the molecular diversity of Type II crustins in penaeids, we identified and characterized a Type IIb crustin in Litopenaeus vannamei (Crustin-like Lv) and compared Type II crustins at both molecular and transcriptional levels. Although L. vannamei Type II crustins (Crustin Lv and Crustin-like Lv) are encoded by separate genes, they showed a similar tissue distribution (hemocytes and gills) and transcriptional response to the shrimp pathogens Vibrio harveyi and White spot syndrome virus (WSSV). As Crustin Lv, Crustin-like Lv transcripts were found to be present early in development, suggesting a maternal contribution to shrimp progeny. Altogether, our in silico and transcriptional data allowed to conclude that (1) each sub-type displays a specific amino acid signature at the C-terminal end holding both the cysteine-rich region and the whey acidic protein (WAP) domain, and that (2) shrimp Type II crustins evolved from a common ancestral gene that conserved a similar pattern of transcriptional regulation.

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“…The number of glycines varies between species but is usually between 20 and 50, and in shrimp is often arranged as repeat VGGGLG motifs that vary in number from 5 to 8 [12,38,[40][41][42][43][44]. Type II crustins were the second type to be described [12] and occur mainly in shrimp (Dendrobrachiata).…”

Section: Crustin Typesmentioning

confidence: 99%

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Smith

Fernandes²,

Kemp

et al. 2008

Developmental & Comparative Immunology

243

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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Molecular cloning of crustins from the hemocytes of Brazilian penaeid shrimps

Cited by 31 publications

References 11 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

Specific Molecular Signatures for Type II Crustins in Penaeid Shrimp Uncovered by the Identification of Crustin-Like Antimicrobial Peptides in Litopenaeus vannamei

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

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