Novel antimicrobial anionic cecropins from the spruce budworm feature a poly-L-aspartic acid C-terminus.


Journal

Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181

Informations de publication

Date de publication:
09 2021
Historique:
revised: 28 04 2021
received: 16 07 2020
accepted: 06 05 2021
pubmed: 12 5 2021
medline: 5 2 2022
entrez: 11 5 2021
Statut: ppublish

Résumé

Cecropins form a family of amphipathic α-helical cationic peptides with broad-spectrum antibacterial properties and potent anticancer activity. The emergence of bacteria and cancer cells showing resistance to cationic antimicrobial peptides (CAMPs) has fostered a search for new, more selective and more effective alternatives to CAMPs. With this goal in mind, we looked for cecropin homologs in the genome and transcriptome of the spruce budworm, Choristoneura fumiferana. Not only did we find paralogs of the conventional cationic cecropins (Cfcec

Identifiants

pubmed: 33973678
doi: 10.1002/prot.26142
doi:

Substances chimiques

Anti-Bacterial Agents 0
Antineoplastic Agents 0
BCL2 protein, human 0
Cecropins 0
Insect Proteins 0
Peptides 0
Proto-Oncogene Proteins c-bcl-2 0
polyaspartate 26063-13-8

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1205-1215

Subventions

Organisme : CIHR
Pays : Canada

Informations de copyright

© 2021 Wiley Periodicals LLC.

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Auteurs

Halim Maaroufi (H)

Institut de biologie intégrative et des systèmes (IBIS), Université Laval, Quebec City, Canada.

Marianne Potvin (M)

Institut de biologie intégrative et des systèmes (IBIS), Université Laval, Quebec City, Canada.

Michel Cusson (M)

Natural Resources Canada, Canadian Forest Service, Laurentian Forestry Centre, Quebec City, Canada.

Roger C Levesque (RC)

Institut de biologie intégrative et des systèmes (IBIS) and Faculté de médecine, Université Laval, Quebec City, Canada.

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