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Registro Completo |
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
27/03/2025 |
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Data da última atualização: |
27/03/2025 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
ORFANOUDAKI, M.; KRUMPE, L. R. H.; SHENOY, S. R.; WILSON, J.; GUSZCZYNSKI, T.; HENRICH, C. J.; TEMME, J. S.; GILDERSLEEVE, J. C.; MOLINA-MOLINA, E.; ERKIZIA, I.; BLANCO, J.; IZQUIERDO-USEROS, N.; MONTIERO, F.; TANURI, A.; RECH FILHO, E. L.; O’KEEFE, B. R. |
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Afiliação: |
MARIA ORFANOUDAKI, NATIONAL CANCER INSTITUTE; LAUREN R. H. KRUMPE, NATIONAL CANCER INSTITUTE; SHILPA R. SHENOY, NATIONAL CANCER INSTITUTE; JENNIFER WILSON, NATIONAL CANCER INSTITUTE; TAD GUSZCZYNSKI, NATIONAL CANCER INSTITUTE; CURTIS J. HENRICH, NATIONAL CANCER INSTITUTE; J. SEBASTIAN TEMME, NATIONAL CANCER INSTITUTE; JEFFREY C. GILDERSLEEVE, NATIONAL CANCER INSTITUTE; ELISA MOLINA-MOLINA, UNIVERSITAT AUTÒNOMA DE BARCELONA (UAB); ITZIAR ERKIZIA, UNIVERSITAT AUTÒNOMA DE BARCELONA (UAB); JULIÀ BLANCO, UNIVERSITAT AUTÒNOMA DE BARCELONA (UAB); NURIA IZQUIERDO-USEROS, UNIVERSITAT AUTÒNOMA DE BARCELONA (UAB); FABIO MONTIERO, INSTITUTE OF SCIENCE AND TECHNOLOGY IN SYNTHETIC BIOLOGY; AMILCAR TANURI, INSTITUTE OF SCIENCE AND TECHNOLOGY IN SYNTHETIC BIOLOGY; ELIBIO LEOPOLDO RECH FILHO, CENARGEN; BARRY R. O’KEEFE, NATIONAL CANCER INSTITUTE. |
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Título: |
Isolation and structure elucidation of Dm-CVNH, a new cyanovirin-N homolog with activity against SARS-CoV-2 and HIV-1. |
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Ano de publicação: |
2025 |
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Fonte/Imprenta: |
Journal of Biological Chemistry, v. 301, n. 3, 108319, 2025. |
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Idioma: |
Português |
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Notas: |
Na publicação: Elibio Rech. |
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Conteúdo: |
An anti-HIV screen of natural product extracts resulted in the discovery of a new antiviral protein through bioassay-guided fractionation of an aqueous extract of the ascidian Didemnum molle. The protein was sequenced through a combination of tandem mass spectroscopy and N-terminal Edman degradation of peptide fragments after a series of endoproteinase digestions. The primary amino acid sequence and disulfide bonding pattern of the 102-amino acid protein were closely related to the antiviral protein cyanovirin-N (CV-N). This new CV-N homolog was named Dm-CVNH. Alphafold2 prediction resulted in a tertiary structure, highly similar to CV-N, comprised of two symmetrically related domains that contained five β-strands and two α-helical turns each. Dm-CVNH showed specificity for high mannose and oligomannose structures, bound to HIV-1 gp-120 and potently inactivated HIV in neutralization assays (EC50 of 0.95 nM). Dm-CVNH inhibited infection in a SARS-CoV-2 live virus assays and was shown to bind to the S1 domain of SARS-CoV-2 Spike glycoprotein. Dm-CVNH behaved in a manner similar to CV-N, binding with a 2:1 stoichiometry to Spike (both to WH-1 and Omicron variants) and preferring the Omicron variant (Kd 42 nM) to original WH-1 (Kd = 89 nM) Spike. This sensitivity to emergent strains was mirrored in viral neutralization assays where Dm-CVNH potently inhibited the infection of Omicron strains XBB.1.16 and JN.1 (IC50 = 11–18 nM). |
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Palavras-Chave: |
Antiviral; Cyanovirin-N homolog; Didemnum molle; HIV; Lectin; Natural product; SARS-CoV-2. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02586naa a2200397 a 4500
001 2174261
005 2025-03-27
008 2025 bl uuuu u00u1 u #d
100 1 $aORFANOUDAKI, M.
245 $aIsolation and structure elucidation of Dm-CVNH, a new cyanovirin-N homolog with activity against SARS-CoV-2 and HIV-1.$h[electronic resource]
260 $c2025
500 $aNa publicação: Elibio Rech.
520 $aAn anti-HIV screen of natural product extracts resulted in the discovery of a new antiviral protein through bioassay-guided fractionation of an aqueous extract of the ascidian Didemnum molle. The protein was sequenced through a combination of tandem mass spectroscopy and N-terminal Edman degradation of peptide fragments after a series of endoproteinase digestions. The primary amino acid sequence and disulfide bonding pattern of the 102-amino acid protein were closely related to the antiviral protein cyanovirin-N (CV-N). This new CV-N homolog was named Dm-CVNH. Alphafold2 prediction resulted in a tertiary structure, highly similar to CV-N, comprised of two symmetrically related domains that contained five β-strands and two α-helical turns each. Dm-CVNH showed specificity for high mannose and oligomannose structures, bound to HIV-1 gp-120 and potently inactivated HIV in neutralization assays (EC50 of 0.95 nM). Dm-CVNH inhibited infection in a SARS-CoV-2 live virus assays and was shown to bind to the S1 domain of SARS-CoV-2 Spike glycoprotein. Dm-CVNH behaved in a manner similar to CV-N, binding with a 2:1 stoichiometry to Spike (both to WH-1 and Omicron variants) and preferring the Omicron variant (Kd 42 nM) to original WH-1 (Kd = 89 nM) Spike. This sensitivity to emergent strains was mirrored in viral neutralization assays where Dm-CVNH potently inhibited the infection of Omicron strains XBB.1.16 and JN.1 (IC50 = 11–18 nM).
653 $aAntiviral
653 $aCyanovirin-N homolog
653 $aDidemnum molle
653 $aHIV
653 $aLectin
653 $aNatural product
653 $aSARS-CoV-2
700 1 $aKRUMPE, L. R. H.
700 1 $aSHENOY, S. R.
700 1 $aWILSON, J.
700 1 $aGUSZCZYNSKI, T.
700 1 $aHENRICH, C. J.
700 1 $aTEMME, J. S.
700 1 $aGILDERSLEEVE, J. C.
700 1 $aMOLINA-MOLINA, E.
700 1 $aERKIZIA, I.
700 1 $aBLANCO, J.
700 1 $aIZQUIERDO-USEROS, N.
700 1 $aMONTIERO, F.
700 1 $aTANURI, A.
700 1 $aRECH FILHO, E. L.
700 1 $aO’KEEFE, B. R.
773 $tJournal of Biological Chemistry$gv. 301, n. 3, 108319, 2025.
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Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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