Structural Polypeptides of Measles Virus

Tyrrell, D. L. J.; Norrby, Erling

doi:10.1099/0022-1317-39-2-219

Cited by 145 publications

(99 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Furthermore, the size of these proteins corresponds to major N protein degradation products (Croce et al, 1980). Cellular actin (Mr 43K) has been associated with MV NC budding (Bohn et al, 1986) and has been isolated from intact MV virions (Tyrrell & Norrby, 1978). However, it is not a good candidate for the element imparting the granular coat because the association between actin and budding NC is mediated by binding to the viral M protein (Giuffre et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Canine Distemper Virus Nucleocapsid Variants

Oglesbee¹,

Tatalick²,

Rice

et al. 1989

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYNucleocapsid (NC) variants expressed by the Onderstepoort strain of canine distemper virus (CDV) were ultrastructurally and biochemically characterized. Three isolated variants were defined which corresponded to the three variants observed within the cytoplasm of infected cells. Dense NC (D-NC), isolated on discontinuous caesium chloride (CsCI) isopycnic gradients, had an average density of 1.2971 + 0.0042 g/ml. Ultrastructurally, D-NC were 1620.0 + 112.1 nm in length with a 20.1 _+ 1-3 nm outer and a 5.8 + 0.7 nm inner core diameter. The D-NC protein composition was 89-7 ~ of a 61K protein (N), 8-4 ~ of a 75K protein (P) and 1-9 ~o of a 160K to 200K protein (L). A single species of nucleic acid, 15 kb in length, was isolated from D-NC. Light NC (L-NC), similarly isolated, had an average density of 1-2894+0-0040g/ml. L-NC differed ultrastructurally from D-NC in that poor resolution of NC subunits, a larger outer diameter (32.0 + 2.8 nm), and a greater inner core diameter (10.4 + 0.6 nm) were observed. The average L-NC strand length was 1574.4 + 115.8 nm. The protein composition was the same as D-NC with the exception of an additional 70K protein, representing 4.0 to 7.7 ~ of the total L-NC protein mass. A 15 kb nucleic acid was also identified in L-NC, although heightened sensitivity of encapsidated L-NC nucleic acid to non-specific nuclease degradation was observed. The ratio of D-NC to L-NC isolated from individual virus preparations varied and was independent of viral infectivity. A third NC variant, defective-NC (Df-NC), was also identified. This had the lowest density on CsC1 gradients (1.2460 + 0.0046 g/ml). The Df-NC structures were truncated to a uniform length of 87.0 + 5.8 nm. Diameter measurements were between those of D-NC and L-NC, being 24.4 + 1-4 nm (outer) and 6.9 + 0.4 nm (inner core). Like L-NC, the 70K protein was present but in greater amounts, representing as much as 43-7~ of the total Df-NC protein mass. RNase A-sensitive nucleic acid was isolated from Df-NC which ranged in size from 1.16 to 0-67 kb with a majority of the material being 0.86 kb in length. For both L-NC and Df-NC, canine CDV convalescent serum reacted with viral N and P proteins in Western blot analyses but not with the 70K protein, suggesting a host cellular origin for the latter.

show abstract

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Canine Distemper Virus Nucleocapsid Variants

Oglesbee¹,

Tatalick²,

Rice

et al. 1989

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…The biological activity of the F protein is generated by cleavage into a non-glycosylated F1 and a glycosylated F2 part (l~ardwick & Bussell, 1978;Tyrrell & Norrby, 1978)joined together by disulphide bridges. Monoclonal antibodies against the F protein do not reveal any variations in epitopes on this component in different strains (Sheshberadaran et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

“…The cytoplasmic membrane of infected cells and the virion envelope contain two surface glycoproteins, the haemagglutinin (H) and fusion (F) proteins, and the non-glycosylated matrix (M) protein, forming the inner layer of the envelope (Mountcastle & Choppin, 1977;Tyrrell & Norrby, 1978 ;Fujinami et al, 1981). The haemagglutinin represents the major surface antigen and thus is the main component for immune recognition of measles virus.…”

Section: Introductionmentioning

confidence: 99%

Purification, Morphology and Antigenic Characterization of Measles Virus Envelope Components

Varsànyi

Utter

Norrby

1984

Journal of General Virology

Self Cite

View full text Add to dashboard Cite

SUMMARYMeasles virus haemagglutinin (H), fusion (F) and matrix (M) components were purified by affinity chromatography using monoclonal antibodies coupled to CNBractivated Sepharose. H and M proteins were purified to homogeneity as determined by polyacrylamide gel electrophoresis by a single cycle of adsorption-desorption. The corresponding purification of the F protein required two cycles of adsorptiondesorption. After the second adsorption an extra wash with 1 M-guanidine-HCl was employed to remove the contaminating cellular actin. Electron microscopic examination of the purified envelope proteins showed that, at pH 6.0, the H peplomers had a truncated conical shape (width 6.5 to 4 nm, length 16 nm), and the F peplomers had a club-like shape (dimensions of the oval head 6 x 9 nm, length 15 nm). Lengths of both peplomers were measured excluding their undiscernible hydrophobic part. The M component at pH 3-0 appeared as a rounded particle (diam. 8 nm, central accumulation of contrast 1.5 nm) suggested to include four to six M polypeptides. Rabbit hyperimmune sera were prepared against all three purified envelope components. These sera reacted only with the homologous antigen in radioimmunoprecipitation assays. Both antisera against the H and F components neutralized the virus and blocked virus-specific haemolysis, but only anti-H serum inhibited haemagglutination.

show abstract

“…Measles virus HA and haemolysin (HL) are antigenically distinct (Norrby & Gollmar, 1975) and the HL is more sensitive than HA to thermal inactivation, treatment with formalin, ether, or Tween 80 ether (Norrby & Falksveden, 1964;Norrby & Gollmar, 1975). Biochemical evidence suggests that measles virus HA and HL are separate polypeptides (Tyrrell & Norrby, 1978;Hardwick & Bussell, 1976), but little is known of the structural arrangement of these antigens within the virion envelope. Trypsin treatment of purified measles virions has been shown to remove the spikes from the particles (Norrby & Gollmar, 1975) and antiserum prepared against purified haemagglutinin of measles virus failed to react with cells persistently infected with measles virus which had been treated with trypsin (Fraser et al, 1978.…”

Section: Discussionmentioning

confidence: 99%