DOI: 10.1073/pnas.85.14.5195. Identification of two integral membrane proteins of Plasmodium falciparum.

Identification of two integral membrane proteins of Plasmodium falciparum.

10.1073/pnas.85.14.5195

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

We describe the isolation and cloning of two integral membrane protein antigens of Plasmodium falciparum. The antigens were isolated by Triton X-114 temperature-dependent phase separation, electrophoretically transferred to nitrocellulose, and used to affinity-purify monospecific human antibodies. These antibodies were used to isolate the corresponding cDNA clones from a phage lambda gt11-Amp3 cDNA expression library. Clone Ag512 corresponds to a Mr 55,000 merozoite rhoptry antigen, and clone Ag513 corresponds to a Mr 45,000 merozoite surface antigen. Both proteins can be biosynthetically labeled with [3H]glucosamine and [3H]myristic acid, suggesting that they may be anchored in membranes via a glycosylphosphatidylinositol moiety. Similarities in the C-terminal sequences of the Mr 45,000 merozoite surface antigen and the Trypanosoma brucei variant surface glycoproteins provides further evidence that this antigen has a glycosylphosphatidylinositol anchor.

Bibliography

Smythe, J. A., Coppel, R. L., Brown, G. V., Ramasamy, R., Kemp, D. J., & Anders, R. F. (1988). Identification of two integral membrane proteins of Plasmodium falciparum. Proceedings of the National Academy of Sciences, 85(14), 5195â5199.

Authors 6

J A Smythe (first)
R L Coppel (additional)
G V Brown (additional)
R Ramasamy (additional)
D J Kemp (additional)
R F Anders (additional)

References 0 Referenced 152

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 6:38 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:55 p.m.)
Indexed	3 months, 1 week ago (May 22, 2025, 8:06 a.m.)
Issued	37 years, 2 months ago (July 1, 1988)
Published	37 years, 2 months ago (July 1, 1988)
Published Online	37 years, 2 months ago (July 1, 1988)
Published Print	37 years, 2 months ago (July 1, 1988)

Funders 0

None

BibTeX

@article{Smythe_1988, title={Identification of two integral membrane proteins of Plasmodium falciparum.}, volume={85}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.85.14.5195}, DOI={10.1073/pnas.85.14.5195}, number={14}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Smythe, J A and Coppel, R L and Brown, G V and Ramasamy, R and Kemp, D J and Anders, R F}, year={1988}, month=jul, pages={5195–5199} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        5,
        22
      ]
    ],
    "date-time": "2025-05-22T12:06:50Z",
    "timestamp": 1747915610912
  },
  "reference-count": 0,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "14",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1988,
        7
      ]
    ]
  },
  "abstract": "<jats:p>We describe the isolation and cloning of two integral membrane protein antigens of Plasmodium falciparum. The antigens were isolated by Triton X-114 temperature-dependent phase separation, electrophoretically transferred to nitrocellulose, and used to affinity-purify monospecific human antibodies. These antibodies were used to isolate the corresponding cDNA clones from a phage lambda gt11-Amp3 cDNA expression library. Clone Ag512 corresponds to a Mr 55,000 merozoite rhoptry antigen, and clone Ag513 corresponds to a Mr 45,000 merozoite surface antigen. Both proteins can be biosynthetically labeled with [3H]glucosamine and [3H]myristic acid, suggesting that they may be anchored in membranes via a glycosylphosphatidylinositol moiety. Similarities in the C-terminal sequences of the Mr 45,000 merozoite surface antigen and the Trypanosoma brucei variant surface glycoproteins provides further evidence that this antigen has a glycosylphosphatidylinositol anchor.</jats:p>",
  "DOI": "10.1073/pnas.85.14.5195",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        5,
        31
      ]
    ],
    "date-time": "2006-05-31T10:38:36Z",
    "timestamp": 1149071916000
  },
  "page": "5195-5199",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 152,
  "title": "Identification of two integral membrane proteins of Plasmodium falciparum.",
  "prefix": "10.1073",
  "volume": "85",
  "author": [
    {
      "given": "J A",
      "family": "Smythe",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    },
    {
      "given": "R L",
      "family": "Coppel",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    },
    {
      "given": "G V",
      "family": "Brown",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    },
    {
      "given": "R",
      "family": "Ramasamy",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    },
    {
      "given": "D J",
      "family": "Kemp",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    },
    {
      "given": "R F",
      "family": "Anders",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia."
        }
      ]
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        1988,
        7
      ]
    ]
  },
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.85.14.5195",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        13
      ]
    ],
    "date-time": "2022-04-13T16:55:59Z",
    "timestamp": 1649868959000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.85.14.5195"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1988,
        7
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "14",
    "published-print": {
      "date-parts": [
        [
          1988,
          7
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.85.14.5195"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.85.14.5195",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        1988,
        7
      ]
    ]
  },
  "assertion": [
    {
      "value": "1988-07-01",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}