DOI: 10.1128/aac.41.7.1521. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development

Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development

10.1128/aac.41.7.1521

Crossref journal-article

American Society for Microbiology

Antimicrobial Agents and Chemotherapy (235)

Abstract

We have isolated and sequenced a novel 11-kDa virucidal protein, named cyanovirin-N (CV-N), from cultures of the cyanobacterium (blue-green alga) Nostoc ellipsosporum. We also have produced CV-N recombinantly by expression of a corresponding DNA sequence in Escherichia coli. Low nanomolar concentrations of either natural or recombinant CV-N irreversibly inactivate diverse laboratory strains and primary isolates of human immunodeficiency virus (HIV) type 1 as well as strains of HIV type 2 and simian immunodeficiency virus. In addition, CV-N aborts cell-to-cell fusion and transmission of HIV-1 infection. Continuous, 2-day exposures of uninfected CEM-SS cells or peripheral blood lymphocytes to high concentrations (e.g., 9,000 nM) of CV-N were not lethal to these representative host cell types. The antiviral activity of CV-N is due, at least in part, to unique, high-affinity interactions of CV-N with the viral surface envelope glycoprotein gp120. The biological activity of CV-N is highly resistant to physicochemical denaturation, further enhancing its potential as an anti-HIV microbicide.

Bibliography

Boyd, M. R., Gustafson, K. R., McMahon, J. B., Shoemaker, R. H., OâKeefe, B. R., Mori, T., Gulakowski, R. J., Wu, L., Rivera, M. I., Laurencot, C. M., Currens, M. J., Cardellina, J. H., Buckheit, R. W., Nara, P. L., Pannell, L. K., Sowder, R. C., & Henderson, L. E. (1997). Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development. Antimicrobial Agents and Chemotherapy, 41(7), 1521â1530.

Authors 17

M R Boyd (first)
K R Gustafson (additional)
J B McMahon (additional)
R H Shoemaker (additional)
B R O'Keefe (additional)
T Mori (additional)
R J Gulakowski (additional)
L Wu (additional)
M I Rivera (additional)
C M Laurencot (additional)
M J Currens (additional)
J H Cardellina (additional)
R W Buckheit (additional)
P L Nara (additional)
L K Pannell (additional)
R C Sowder (additional)
L E Henderson (additional)

References 0 Referenced 499

None

Dates

Type	When
Created	6 years, 10 months ago (Oct. 8, 2018, 8:28 p.m.)
Deposited	3 years, 6 months ago (Feb. 21, 2022, 3:11 p.m.)
Indexed	1 day, 3 hours ago (Aug. 26, 2025, 2:37 a.m.)
Issued	28 years, 1 month ago (July 1, 1997)
Published	28 years, 1 month ago (July 1, 1997)
Published Print	28 years, 1 month ago (July 1, 1997)

Funders 0

None

BibTeX

@article{Boyd_1997, title={Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development}, volume={41}, ISSN={1098-6596}, url={http://dx.doi.org/10.1128/aac.41.7.1521}, DOI={10.1128/aac.41.7.1521}, number={7}, journal={Antimicrobial Agents and Chemotherapy}, publisher={American Society for Microbiology}, author={Boyd, M R and Gustafson, K R and McMahon, J B and Shoemaker, R H and O’Keefe, B R and Mori, T and Gulakowski, R J and Wu, L and Rivera, M I and Laurencot, C M and Currens, M J and Cardellina, J H and Buckheit, R W and Nara, P L and Pannell, L K and Sowder, R C and Henderson, L E}, year={1997}, month=jul, pages={1521–1530} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        26
      ]
    ],
    "date-time": "2025-08-26T06:37:29Z",
    "timestamp": 1756190249124
  },
  "reference-count": 0,
  "publisher": "American Society for Microbiology",
  "issue": "7",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            1997,
            7,
            1
          ]
        ],
        "date-time": "1997-07-01T00:00:00Z",
        "timestamp": 867715200000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://journals.asm.org/non-commercial-tdm-license"
    }
  ],
  "content-domain": {
    "domain": [
      "journals.asm.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1997,
        7
      ]
    ]
  },
  "abstract": "<jats:p>We have isolated and sequenced a novel 11-kDa virucidal protein, named cyanovirin-N (CV-N), from cultures of the cyanobacterium (blue-green alga) Nostoc ellipsosporum. We also have produced CV-N recombinantly by expression of a corresponding DNA sequence in Escherichia coli. Low nanomolar concentrations of either natural or recombinant CV-N irreversibly inactivate diverse laboratory strains and primary isolates of human immunodeficiency virus (HIV) type 1 as well as strains of HIV type 2 and simian immunodeficiency virus. In addition, CV-N aborts cell-to-cell fusion and transmission of HIV-1 infection. Continuous, 2-day exposures of uninfected CEM-SS cells or peripheral blood lymphocytes to high concentrations (e.g., 9,000 nM) of CV-N were not lethal to these representative host cell types. The antiviral activity of CV-N is due, at least in part, to unique, high-affinity interactions of CV-N with the viral surface envelope glycoprotein gp120. The biological activity of CV-N is highly resistant to physicochemical denaturation, further enhancing its potential as an anti-HIV microbicide.</jats:p>",
  "DOI": "10.1128/aac.41.7.1521",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2018,
        10,
        9
      ]
    ],
    "date-time": "2018-10-09T00:28:57Z",
    "timestamp": 1539044937000
  },
  "page": "1521-1530",
  "update-policy": "http://dx.doi.org/10.1128/asmj-crossmark-policy-page",
  "source": "Crossref",
  "is-referenced-by-count": 499,
  "title": "Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development",
  "prefix": "10.1128",
  "volume": "41",
  "author": [
    {
      "given": "M R",
      "family": "Boyd",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "K R",
      "family": "Gustafson",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "J B",
      "family": "McMahon",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "R H",
      "family": "Shoemaker",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "B R",
      "family": "O'Keefe",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "T",
      "family": "Mori",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "R J",
      "family": "Gulakowski",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "L",
      "family": "Wu",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "M I",
      "family": "Rivera",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "C M",
      "family": "Laurencot",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "M J",
      "family": "Currens",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "suffix": "2nd",
      "given": "J H",
      "family": "Cardellina",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "suffix": "Jr",
      "given": "R W",
      "family": "Buckheit",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "P L",
      "family": "Nara",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "L K",
      "family": "Pannell",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "suffix": "2nd",
      "given": "R C",
      "family": "Sowder",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    },
    {
      "given": "L E",
      "family": "Henderson",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Division of Cancer Treatment, Diagnosis and Centers, National Cancer Institute, Frederick, Maryland 21702-1201, USA. boyd@dtpax2.ncifcrf.gov"
        }
      ]
    }
  ],
  "member": "235",
  "container-title": "Antimicrobial Agents and Chemotherapy",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://journals.asm.org/doi/pdf/10.1128/AAC.41.7.1521",
      "content-type": "application/pdf",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://journals.asm.org/doi/pdf/10.1128/AAC.41.7.1521",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        2,
        21
      ]
    ],
    "date-time": "2022-02-21T20:11:29Z",
    "timestamp": 1645474289000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://journals.asm.org/doi/10.1128/AAC.41.7.1521"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1997,
        7
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "7",
    "published-print": {
      "date-parts": [
        [
          1997,
          7
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1128/AAC.41.7.1521"
  ],
  "URL": "http://dx.doi.org/10.1128/AAC.41.7.1521",
  "relation": {},
  "ISSN": [
    "0066-4804",
    "1098-6596"
  ],
  "subject": [],
  "container-title-short": "Antimicrob Agents Chemother",
  "published": {
    "date-parts": [
      [
        1997,
        7
      ]
    ]
  },
  "assertion": [
    {
      "value": "1997-07-01",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}