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Protein

Cyanovirin-N

Gene
N/A
Organism
Nostoc ellipsosporum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mannose-binding lectin.2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB

GO - Biological processi

  • regulation of defense response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antiviral protein

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Cyanovirin-N
Short name:
CV-N
OrganismiNostoc ellipsosporum
Taxonomic identifieri45916 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Pathology & Biotechi

Biotechnological usei

Overexpression of this protein to provide quantities adequate for medical use as a topical microbiocide has been attempted in a number of systems including E.coli (PubMed:9210678, PubMed:19547966), Lactobacillus jensenii (PubMed:17005802), the yeast Pichia pastoris (PubMed:12356469) and Nicotiana tabacum (PubMed:16354721); see PubMed:20162270 for a review.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301N → A, Q or V: Prevents N-glycosylation upon overexpression in yeast without changing anti-HIV activity. 1 Publication
Mutagenesisi51 – 511P → G: Protein is mostly monomeric and has wild-type anti-HIV activity. 1 Publication
Mutagenesisi52 – 521S → P: Protein is exclusively dimeric and has moderate anti-HIV activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Cyanovirin-NPRO_0000079579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi8 ↔ 221 Publication
Disulfide bondi58 ↔ 731 Publication

Post-translational modificationi

Cleavage, or reduction and alkylation of the disulfide bonds results in the loss of anti-HIV activity.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

In solution exists as a metastable domain-swapped homodimer which very slowly converts into a more stable monomeric form at room temperature. Under physiological conditions it is unlikely that the dimeric species exists and indeed the monomer is more active against HIV. Interacts with HIV-1 gp120.3 Publications

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi8 – 147Combined sources
Beta strandi17 – 237Combined sources
Beta strandi27 – 359Combined sources
Turni37 – 393Combined sources
Beta strandi40 – 434Combined sources
Beta strandi46 – 483Combined sources
Helixi54 – 563Combined sources
Beta strandi58 – 647Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 747Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 867Combined sources
Helixi87 – 893Combined sources
Beta strandi91 – 944Combined sources
Beta strandi97 – 1004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IIYNMR-A1-101[»]
1J4VNMR-A/B1-101[»]
1L5BX-ray2.00A/B1-101[»]
1L5ENMR-A/B1-101[»]
1LOMX-ray1.72A1-101[»]
1N02NMR-A1-101[»]
2EZMNMR-A1-101[»]
2EZNNMR-A1-101[»]
2PYSX-ray1.80A/B1-101[»]
2RDKX-ray1.35A/B1-101[»]
2RP3NMR-A1-101[»]
2Z21X-ray1.80A/B1-101[»]
3CZZX-ray1.36A/B1-101[»]
3EZMX-ray1.50A1-101[»]
3GXYX-ray2.40A/B1-101[»]
3GXZX-ray2.50A/B1-101[»]
3LHCX-ray1.34A1-101[»]
3S3YX-ray2.00A1-101[»]
3S3ZX-ray1.75A1-101[»]
4J4CX-ray1.90A1-101[»]
4J4DX-ray2.00A/B/C/D1-101[»]
4J4EX-ray2.40A/B/C/D/E/F1-101[»]
4J4FX-ray1.90A/B/C/D1-101[»]
4J4GX-ray1.92A/B/C/D1-101[»]
ProteinModelPortaliP81180.
SMRiP81180. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81180.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyanovirin-N family.Curated

Family and domain databases

Gene3Di2.30.60.10. 1 hit.
InterProiIPR011058. Cyanovirin-N.
[Graphical view]
PfamiPF08881. CVNH. 1 hit.
[Graphical view]
SMARTiSM01111. CVNH. 1 hit.
[Graphical view]
SUPFAMiSSF51322. SSF51322. 1 hit.

Sequencei

Sequence statusi: Complete.

P81180-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LGKFSQTCYN SAIQGSVLTS TCERTNGGYN TSSIDLNSVI ENVDGSLKWQ
60 70 80 90 100
PSNFIETCRN TQLAGSSELA AECKTRAQQF VSTKINLDDH IANIDGTLKY

E
Length:101
Mass (Da):11,013
Last modified:December 1, 2000 - v2
Checksum:i1F8FA5B88ACCE57F
GO

Mass spectrometryi

Molecular mass is 11014.2 Da from positions 1 - 101. Determined by ESI. 1 Publication

Sequence databases

PIRiJC5631.

Cross-referencesi

Sequence databases

PIRiJC5631.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IIYNMR-A1-101[»]
1J4VNMR-A/B1-101[»]
1L5BX-ray2.00A/B1-101[»]
1L5ENMR-A/B1-101[»]
1LOMX-ray1.72A1-101[»]
1N02NMR-A1-101[»]
2EZMNMR-A1-101[»]
2EZNNMR-A1-101[»]
2PYSX-ray1.80A/B1-101[»]
2RDKX-ray1.35A/B1-101[»]
2RP3NMR-A1-101[»]
2Z21X-ray1.80A/B1-101[»]
3CZZX-ray1.36A/B1-101[»]
3EZMX-ray1.50A1-101[»]
3GXYX-ray2.40A/B1-101[»]
3GXZX-ray2.50A/B1-101[»]
3LHCX-ray1.34A1-101[»]
3S3YX-ray2.00A1-101[»]
3S3ZX-ray1.75A1-101[»]
4J4CX-ray1.90A1-101[»]
4J4DX-ray2.00A/B/C/D1-101[»]
4J4EX-ray2.40A/B/C/D/E/F1-101[»]
4J4FX-ray1.90A/B/C/D1-101[»]
4J4GX-ray1.92A/B/C/D1-101[»]
ProteinModelPortaliP81180.
SMRiP81180. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81180.

Family and domain databases

Gene3Di2.30.60.10. 1 hit.
InterProiIPR011058. Cyanovirin-N.
[Graphical view]
PfamiPF08881. CVNH. 1 hit.
[Graphical view]
SMARTiSM01111. CVNH. 1 hit.
[Graphical view]
SUPFAMiSSF51322. SSF51322. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development."
    Boyd M.R., Gustafson K.R., McMahon J.B., Shoemaker R.H., O'Keefe B.R., Mori T., Gulakowski R.J., Wu L., Rivera M.I., Laurencot C.M., Currens M.J., Cardellina J.H. II, Buckheit R.W. Jr., Nara P.L., Pannell L.K., Sowder R.C. II, Henderson L.E.
    Antimicrob. Agents Chemother. 41:1521-1530(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, STABILITY, BIOTECHNOLOGY (EXPRESSION IN E.COLI), INTERACTION WITH HIV-1 GP120.
  2. "Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum."
    Gustafson K.R., Sowder R.C. II, Henderson L.E., Cardellina J.H. II, McMahon J.B., Rajamani U., Pannell L.K., Boyd M.R.
    Biochem. Biophys. Res. Commun. 238:223-228(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, DISULFIDE BOND.
  3. "Multiple antiviral activities of cyanovirin-N: blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses."
    Dey B., Lerner D.L., Lusso P., Boyd M.R., Elder J.H., Berger E.A.
    J. Virol. 74:4562-4569(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VIRAL SUBSTRATES.
  4. "Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts."
    Mori T., Barrientos L.G., Han Z., Gronenborn A.M., Turpin J.A., Boyd M.R.
    Protein Expr. Purif. 26:42-49(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY (EXPRESSION IN PICHIA PASTORIS), MUTAGENESIS OF ASN-30.
  5. "Cyanovirin-N: a sugar-binding antiviral protein with a new twist."
    Botos I., Wlodawer A.
    Cell. Mol. Life Sci. 60:277-287(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Engineered vaginal lactobacillus strain for mucosal delivery of the human immunodeficiency virus inhibitor cyanovirin-N."
    Liu X., Lagenaur L.A., Simpson D.A., Essenmacher K.P., Frazier-Parker C.L., Liu Y., Tsai D., Rao S.S., Hamer D.H., Parks T.P., Lee P.P., Xu Q.
    Antimicrob. Agents Chemother. 50:3250-3259(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY (EXPRESSION IN LACTOBACILLUS JENSENII).
  7. "Transgenic plant production of Cyanovirin-N, an HIV microbicide."
    Sexton A., Drake P.M., Mahmood N., Harman S.J., Shattock R.J., Ma J.K.
    FASEB J. 20:356-358(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY (EXPRESSION IN NICOTIANA TABACUM).
  8. "Soluble cytoplasmic expression, rapid purification, and characterization of cyanovirin-N as a His-SUMO fusion."
    Gao X., Chen W., Guo C., Qian C., Liu G., Ge F., Huang Y., Kitazato K., Wang Y., Xiong S.
    Appl. Microbiol. Biotechnol. 85:1051-1060(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY (EXPRESSION IN ESCHERICHIA COLI).
  9. "The antiviral protein cyanovirin-N: the current state of its production and applications."
    Xiong S., Fan J., Kitazato K.
    Appl. Microbiol. Biotechnol. 86:805-812(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Solution structure of cyanovirin-N, a potent HIV-inactivating protein."
    Bewley C.A., Gustafson K.R., Boyd M.R., Covell D.G., Bax A., Clore G.M., Gronenborn A.M.
    Nat. Struct. Biol. 5:571-578(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping."
    Yang F., Bewley C.A., Louis J.M., Gustafson K.R., Boyd M.R., Gronenborn A.M., Clore G.M., Wlodawer A.
    J. Mol. Biol. 288:403-412(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  12. "Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides."
    Botos I., O'Keefe B.R., Shenoy S.R., Cartner L.K., Ratner D.M., Seeberger P.H., Boyd M.R., Wlodawer A.
    J. Biol. Chem. 277:34336-34342(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HIGH-MANNOSE OLIGOSACCHARIDES.
  13. "The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures."
    Barrientos L.G., Louis J.M., Botos I., Mori T., Han Z., O'Keefe B.R., Boyd M.R., Wlodawer A., Gronenborn A.M.
    Structure 10:673-686(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), STRUCTURE BY NMR, SUBUNIT, MUTAGENESIS OF PRO-51 AND SER-52.

Entry informationi

Entry nameiCVN_NOSEL
AccessioniPrimary (citable) accession number: P81180
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: May 11, 2016
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Its activity in situ is unknown, however it acts as a viral entry inhibitor, inhibiting HIV-1, HIV-2 and simian immunodeficiency virus (and some other viruses such as feline immunodeficiency virus, measles virus and human herpesvirus) infection and replication. It prevents essential interactions between the envelope glycoprotein and target cell receptors by binding to carbohydrates on viral protein gp120 and possibly by other mechanisms as well. Addition to cells must occur before or shortly after virus addition. It also inhibits cell-to-cell fusion, and virus-to-cell and cell-to-cell transmission of a viral infection.
Is remarkably stabile; the protein can withstand multiple freeze-thaw cycles, dissolution in organic solvents, treatment with salt, detergent, H2O2 and boiling without significant loss of anti-HIV activity.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.