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AuthorGonzález García, Melainedc.contributor.author
AuthorRodríguez, Armandodc.contributor.author
AuthorAlba, Anniadc.contributor.author
AuthorVázquez, Antonio A.dc.contributor.author
AuthorMorales Vicente, Fidel E.dc.contributor.author
AuthorPérez-Erviti, Juliodc.contributor.author
AuthorSpellerberg, Barbaradc.contributor.author
AuthorStenger, Steffendc.contributor.author
AuthorGrieshober, Markdc.contributor.author
AuthorConzelmann, Carinadc.contributor.author
AuthorMünch, Jandc.contributor.author
AuthorRaber, Heinzdc.contributor.author
AuthorKubiczek, Dennisdc.contributor.author
AuthorRosenau, Frankdc.contributor.author
AuthorWiese, Sebastiandc.contributor.author
AuthorStändker, Ludgerdc.contributor.author
AuthorOtero-González, Anselmodc.contributor.author
Date of accession2021-07-02T08:43:30Zdc.date.accessioned
Available in OPARU since2021-07-02T08:43:30Zdc.date.available
Date of first publication2020-10-23dc.date.issued
AbstractAntimicrobial peptides (AMPs) are biomolecules with antimicrobial activity against a broad group of pathogens. In the past few decades, AMPs have represented an important alternative for the treatment of infectious diseases. Their isolation from natural sources has been widely investigated. In this sense, mollusks are promising organisms for the identification of AMPs given that their immune system mainly relies on innate response. In this report, we characterized the peptide fraction of the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) and identified 37 di erent peptides by nanoLC-ESI-MS-MS technology. From these peptide sequences, using bioinformatic prediction tools, we discovered two potential antimicrobial peptides named Pom-1 (KCAGSIAW AIGSGLFGGAKLIKIKKYIAELGGLQ) and Pom-2 (KEIERAGQRIRDAIISAAPAVETLAQAQKIIKGG). Database search revealed that Pom-1 is a fragment of Closticin 574 previously isolated from the bacteria Clostridium tyrobutyrium, and Pom-2 is a fragment of cecropin D-like peptide first isolated from Galleria mellonella hemolymph. These sequences were chemically synthesized and evaluated against di erent human pathogens. Interestingly, structural predictions of both peptides in the presence of micelles showed models that comprise two alpha helices joined by a short loop. The CD spectra analysis of Pom-1 and Pom-2 in water showed for both structures a high random coil content, a certain content of -helix and a low -sheet content. Like other described AMPs displaying a disordered structure in water, the peptides may adopt a helical conformation in presence of bacterial membranes. In antimicrobial assays, Pom-1 demonstrated high activity against the Gram-negative bacteria Pseudomonas aeruginosa and moderate activity against Klebsiella pneumoniae and Listeria monocytogenes. Neither of the two peptides showed antifungal action. Pom-1 moderately inhibits Zika Virus infection but slightly enhances HIV-1 infectivion in vitro. The evaluation of cell toxicity on primary human macrophages did not show toxicity on THP-1 cells, although slight overall toxicity was observed in high concentrations of Pom-1. We assume that both peptides may play a key role in innate defense of P. poeyana and represent promising antimicrobial candidates for humans.dc.description.abstract
Languageendc.language.iso
PublisherUniversität Ulmdc.publisher
LicenseCC BY 4.0 Internationaldc.rights
Link to license texthttps://creativecommons.org/licenses/by/4.0/dc.rights.uri
KeywordAntimicrobial peptidesdc.subject
KeywordPomacea poeyanadc.subject
KeywordAntibacterial activitydc.subject
Dewey Decimal GroupDDC 570 / Life sciencesdc.subject.ddc
Dewey Decimal GroupDDC 610 / Medicine & healthdc.subject.ddc
LCSHPeptide antibioticsdc.subject.lcsh
LCSHAntibacterial agentsdc.subject.lcsh
TitleNew Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927)dc.title
Resource typeWissenschaftlicher Artikeldc.type
SWORD Date2020-12-09T19:31:43Zdc.date.updated
VersionpublishedVersiondc.description.version
DOIhttp://dx.doi.org/10.18725/OPARU-38134dc.identifier.doi
URNhttp://nbn-resolving.de/urn:nbn:de:bsz:289-oparu-38210-5dc.identifier.urn
GNDPeptidantibiotikumdc.subject.gnd
FacultyFakultät für Naturwissenschaftenuulm.affiliationGeneral
FacultyMedizinische Fakultätuulm.affiliationGeneral
InstitutionKompetenzzentrum "Ulm Peptide Pharmaceuticals (U-PEP)"uulm.affiliationSpecific
InstitutionUKU. Institut für Medizinische Mikrobiologie und Hygieneuulm.affiliationSpecific
InstitutionUKU. Institut für Molekulare Virologieuulm.affiliationSpecific
InstitutionInstitut für Pharmazeutische Biotechnologieuulm.affiliationSpecific
InstitutionCore Unit Mass Spectrometry and Proteomicsuulm.affiliationSpecific
Peer reviewjauulm.peerReview
DCMI TypeTextuulm.typeDCMI
CategoryPublikationenuulm.category
In cooperation withUniversidad de La Habanauulm.cooperation
In cooperation withPedro Kouri National Institute of Tropical Medicineuulm.cooperation
DOI of original publication10.3390/biom10111473dc.relation1.doi
Source - Title of sourceBiomoleculessource.title
Source - Place of publicationMDPIsource.publisher
Source - Volume10source.volume
Source - Issue11source.issue
Source - Year2020source.year
Source - Article number1473source.articleNumber
Source - eISSN2218-273Xsource.identifier.eissn
EU projectFight-nCoV / FIGHTING-OFF CORONAVIRUS (SARS-CoV-2) WITH BROAD-SPECTRUM ANTIVIRALS: ESTABLISHING ANIMAL VIRAL CHALLENGE MODEL / EC / H2020 / 101003555uulm.projectEU
FundingBMBF [DLR CUB 17WTZ-014/01DN18009]uulm.funding
FundingSFB 1279: Exploiting the Human Peptidome for Novel Antimicrobial and Anticancer Agents / DFG [316249678]uulm.funding
Open AccessDOAJ Gold, Green Publisheduulm.OA
WoS000592959000001uulm.identifier.wos
Bibliographyuulmuulm.bibliographie


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