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The protein coat that constitutes the shell of a virus particle.

[From Latin capsa, box.]


(Animals) any heteropterous bug of the family Miridae (formerly Capsidae), most of which feed on plant tissues, causing damage to crops
[C19: from New Latin Capsus (genus)]


(Biochemistry) the outer protein coat of a mature virus
[C20: from French capside, from Latin capsa box]


(ˈkæp sɪd)

the coiled or polyhedral structure, composed of proteins, that encloses the nucleic acid of a virus. Also called protein coat.
[1960–65; < French capside= Latin caps(a) case2 + -ide -id1]
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.capsid - a variety of leaf bugcapsid - a variety of leaf bug    
leaf bug, plant bug - small bright-colored insect that feeds on plant juices
four-lined leaf bug, four-lined plant bug, Poecilocapsus lineatus - yellow or orange leaf bug with four black stripes down the back; widespread in central and eastern North America
lygus bug - vector of viral plant diseases
2.capsid - the outer covering of protein surrounding the nucleic acid of a virus
virion - (virology) a complete viral particle; nucleic acid and capsid (and a lipid envelope in some viruses)
protein - any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
References in periodicals archive ?
The 17 chapters explore simple and complex carbohydrates and glycoconjugates; methods of structural analysis of glycosaminoglycans, applications of these methods for identification of lysosomal storage diseases, and participation in the development of Lyme disease; the role of viral envelope protein glycosylation in the pathogenesis of influenza A virus; the application of lectin histochemistry in the diagnosis of lysosomal storage diseases; computational approaches for studying carbohydrate-lectin interactions in infection; the pathogenic effects of altered sialylation of specific glycoconjugates in genetic diseases; sialyltransferase regulation of cancer-associated O-glycans; and the history of pectin study, chemistry, and medicinal uses of pectin.
But when the virus underwent a mutation in a gene coding for a viral envelope protein, the mutant strain became at least 100-fold more infective for the A.
The first contains the genes that enable the production of key HIV proteins, including the viral envelope protein.