Screening Antimicrobial Activities of Basic Protein Fractions from Dry and Germinated Wheat Seeds

Talas-Oğraş, Tijen

doi:10.1023/b:biop.0000047155.53756.63

Cited by 5 publications

(3 citation statements)

References 23 publications

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“…During the past decade, a large number of antimicrobial proteins have been identified in different plants. Antimicrobial peptides, which constitute a heterogeneous class of low molecular mass proteins, are recognized as important components of the plant defense system (20). These peptides exhibit broad-spectrum activity against a wide range of microorganisms including Gram-positive and Gram-negative bacteria, protozoa, yeast, fungi and viruses.…”

Section: Discussionmentioning

confidence: 99%

A new antimicrobial peptide isolated from Oudneya africana seeds

Hammami

Hamida

Vergoten

et al. 2009

Microbiology and Immunology

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Section: Discussionmentioning

confidence: 99%

A new antimicrobial peptide isolated from Oudneya africana seeds

Hammami

Hamida

Vergoten

et al. 2009

Microbiology and Immunology

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“…Moreover, it sets crustins within their own category of WAP-containing proteins from those found in other taxa [14,[18][19][20][21][22] and distinguishes them from those that have a WAP domain at the N terminus or more than one at the C terminus, even though there may be some functional equivalence between these proteins in terms of their role in inflammation and /or antimicrobial properties [16,23,24,25].…”

Section: Definition Of a Crustinmentioning

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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“…The screening of protein extracts is the initial step of these studies (Talas-Ogras 2004, Cavalheiro et al 2009.…”

Section: Introductionmentioning

confidence: 99%

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Brito

Melo

Alves

et al. 2016

Hoehnea

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-(Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions). The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds. Keywords: antimicrobial, cystatin, Fabaceae, protease RESUMO -(Purificação parcial de um inibidor de tripsina/papaína de sementes de Hymenaea courbaril L. e atividade antibacteriana de suas frações proteicas). O extrato bruto e frações proteicas de sementes de Hymenaea courbaril foram investigados para a presença de inibidores de tripsina e papaína e atividade antimicrobiana contra Vibrio parahaemolyticus, Staphylococcus aureus e Escherichia coli. As frações foram obtidas após precipitação do extrato bruto com sulfato de amônio em três faixas de saturação (0-30%, 30-60% e 60-90%) e denominadas Hc030, Hc3060 e Hc6090, respectivamente. O extrato bruto e as frações apresentaram diferente especificidade em inibir a atividade da tripsina e papaína. A atividade antimicrobiana foi observada nas frações Hc030 e Hc3060 e somente contra V. parahaemolyticus. O inibidor isolado a partir de Hc3060 foi mais eficiente na inibição da tripsina (100% de inibição) do que da papaína (54% de inibição), e mostrou uma massa molecular aparente de 20 kDa. Este estudo mostra que as sementes de H. courbaril possuem inibidores de proteases e proteínas com atividade antibacteriana, indicando que a espécie é uma fonte de compostos bioativos.

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Screening Antimicrobial Activities of Basic Protein Fractions from Dry and Germinated Wheat Seeds

Cited by 5 publications

References 23 publications

A new antimicrobial peptide isolated from Oudneya africana seeds

A new antimicrobial peptide isolated from Oudneya africana seeds

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

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