Properties of the chlorella receptor for the virus PBCV-11

Russel H. Meints; Dwight E. Burbank; James L. Van Etten; Derek T.A. Lamport

doi:10.1016/0042-6822(88)90614-9

Properties of the chlorella receptor for the virus PBCV-11

Russel H. Meints, Dwight E. Burbank, James L. Van Etten, Derek T.A. Lamport

Plant Pathology

Research output: Contribution to journal › Article › peer-review

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Abstract

The virus PBCV-1 attached rapidly, specifically, and irreversibly to the external surface of cell walls of its host, a unicellular, eukaryotic Chlorella-like green alga. Attachment was pH and salt dependent. Each cell contained at least 5 × 10SU PBCV-1 binding sites and Scatchard analysis indicated that each cell could adsorb 5000 PBCV-1 particles. The PBCV-1 receptor was unaffected by extraction with organic solvents, detergents, high salts, or treatment with several proteases as well as the polysaccharide degrading enzymes, cellulase and pectinase. In contrast, acid and alkali treatments of walls at high temperatures and treatment with an enzyme preparation from PBCV-1 lysates destroyed the virus receptor. We suspect that the receptor is a carbohydrate.

Original language	English (US)
Pages (from-to)	15-21
Number of pages	7
Journal	Virology
Volume	164
Issue number	1
DOIs	https://doi.org/10.1016/0042-6822(88)90614-9
State	Published - May 1988

ASJC Scopus subject areas

Virology

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10.1016/0042-6822(88)90614-9

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title = "Properties of the chlorella receptor for the virus PBCV-11",

abstract = "The virus PBCV-1 attached rapidly, specifically, and irreversibly to the external surface of cell walls of its host, a unicellular, eukaryotic Chlorella-like green alga. Attachment was pH and salt dependent. Each cell contained at least 5 × 10SU PBCV-1 binding sites and Scatchard analysis indicated that each cell could adsorb 5000 PBCV-1 particles. The PBCV-1 receptor was unaffected by extraction with organic solvents, detergents, high salts, or treatment with several proteases as well as the polysaccharide degrading enzymes, cellulase and pectinase. In contrast, acid and alkali treatments of walls at high temperatures and treatment with an enzyme preparation from PBCV-1 lysates destroyed the virus receptor. We suspect that the receptor is a carbohydrate.",

author = "Meints, {Russel H.} and Burbank, {Dwight E.} and {Van Etten}, {James L.} and Lamport, {Derek T.A.}",

note = "Funding Information: We thank Joseph Lamport for assistance with the gas chromatography and Myron Brakke and Les Lane for many helpful discussions. This investigation was supported in part by Grant DCB-8417373 from the National Science Foundation (R.H.M.), Grant 85.CRCR-l-1613 from the US. Department of Agriculture (R.H.M.), Contract XK-5-05073-2 from the Solar Energy Research Institute (R.H.M.). and Grant DE AC02-82ER12086 from the Department of Energy (J.V.E.).",

year = "1988",

month = may,

doi = "10.1016/0042-6822(88)90614-9",

language = "English (US)",

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pages = "15--21",

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AU - Meints, Russel H.

AU - Burbank, Dwight E.

AU - Van Etten, James L.

AU - Lamport, Derek T.A.

N1 - Funding Information: We thank Joseph Lamport for assistance with the gas chromatography and Myron Brakke and Les Lane for many helpful discussions. This investigation was supported in part by Grant DCB-8417373 from the National Science Foundation (R.H.M.), Grant 85.CRCR-l-1613 from the US. Department of Agriculture (R.H.M.), Contract XK-5-05073-2 from the Solar Energy Research Institute (R.H.M.). and Grant DE AC02-82ER12086 from the Department of Energy (J.V.E.).

PY - 1988/5

Y1 - 1988/5

N2 - The virus PBCV-1 attached rapidly, specifically, and irreversibly to the external surface of cell walls of its host, a unicellular, eukaryotic Chlorella-like green alga. Attachment was pH and salt dependent. Each cell contained at least 5 × 10SU PBCV-1 binding sites and Scatchard analysis indicated that each cell could adsorb 5000 PBCV-1 particles. The PBCV-1 receptor was unaffected by extraction with organic solvents, detergents, high salts, or treatment with several proteases as well as the polysaccharide degrading enzymes, cellulase and pectinase. In contrast, acid and alkali treatments of walls at high temperatures and treatment with an enzyme preparation from PBCV-1 lysates destroyed the virus receptor. We suspect that the receptor is a carbohydrate.

AB - The virus PBCV-1 attached rapidly, specifically, and irreversibly to the external surface of cell walls of its host, a unicellular, eukaryotic Chlorella-like green alga. Attachment was pH and salt dependent. Each cell contained at least 5 × 10SU PBCV-1 binding sites and Scatchard analysis indicated that each cell could adsorb 5000 PBCV-1 particles. The PBCV-1 receptor was unaffected by extraction with organic solvents, detergents, high salts, or treatment with several proteases as well as the polysaccharide degrading enzymes, cellulase and pectinase. In contrast, acid and alkali treatments of walls at high temperatures and treatment with an enzyme preparation from PBCV-1 lysates destroyed the virus receptor. We suspect that the receptor is a carbohydrate.

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Properties of the chlorella receptor for the virus PBCV-11

Abstract

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