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Journal of General Virology | 1985

Two distinct subtypes of human respiratory syncytial virus.

Maurice A. Mufson; Claes Örvell; Björg Rafnar; Erling Norrby

Antigenic variation of human respiratory syncytial (RS) virus strains was analysed using a collection of nine, six, six, nine and one monoclonal antibodies respectively directed against the large glycoprotein (G), fusion protein (F), matrix protein (M), nucleoprotein (NP) and phosphoprotein (P) components of the Long strain of RS virus. A comparison was made with seven other strains isolated during different years in radioimmune precipitation analyses and immune fluorescence tests. Two different subtypes of the virus were demonstrable. Subtype A included the prototype strains Long and A2 and virus isolates from 1973, 1983 and 1984; subtype B included four virus strains isolated in successive years from 1979 to 1982. Subtype A viruses reacted with all the antibodies, whereas subtype B viruses showed different epitope characteristics in four structural components. The number of altered epitopes were 5/6, 1/2, 2/6 and 1/6 in the G, F, M and NP components, respectively. It is concluded that the two subtypes have evolved separately. The finding of two subtypes may explain previously observed strain variations in neutralization tests, and gives a new perspective on the immunobiology of RS virus.


Experimental Biology and Medicine | 1962

Hemagglutination by Measles Virus. 4. A Simple Procedure for Production of High Potency Antigen for Hemagglutination-Inhibition (HI) Tests.

Erling Norrby

Summary A simple method for increasing hemagglutinating activity of measles virus tissue culture material is described. By treatment with Tween 80 and ether a 4- to 8-fold increase in titer was obtained with virus material grown in a human embryonic cell line (Lu 106) and an 8- to 32-fold increase when virus was grown in dog kidney TC. Maximal HA titers obtained with unconcentrated material were respectively 1:1024 and 1:4096 per 0.4 ml with the two different materials. Serum titers greater by a factor of 2 were obtained when Tween and ether treated material was substituted for untreated material as antigen in HI tests.


Scandinavian Journal of Immunology | 1976

Oligoclonal Measles Virus-Specific IgG Antibodies Isolated from Cerebrospinal Fluids, Brain Extracts, and Sera from Patients with Subacute Sclerosing Panencephalitis and Multiple Sclerosis

Bodvar Vandvik; Erling Norrby; H. J. Nordal; M. Decré

Measles virus‐specific antibodies were isolated from sera, cerebrospinal fluids (CSF), and brain extracts of patients with subacute sclerosing panencephalitis (SSPE) and multiple sclerosis (MS) by absorption with measles antigens and subsequent acid elution of the antigen–antibody precipitates. Electrophoretically homogeneous measles antibodies were isolated from CSF or brain extracts in five patients with SSPE and in five out of seven patients with MS. Homogeneous IgG antibodies were also demonstrated in the sera from all SSPE patients and from three of the MS patients. The antibodies isolated from various control sera and from pooled CSF were electrophoretically heterogeneous. The results support the concept of a local synthesis in the nervous system of oligoclonal IgG antibodies to measles virus in all patients with SSPH and in some patients with MS. In SSPE, most or all oligoclonal IgG proteins of the CSF or brain carry measles antibody activities. In MS, only part of the oligoclonal IgG appears to be associated with measles antibody activity


Journal of General Virology | 1978

Structural polypeptides of measles virus.

David L.J. Tyrrell; Erling Norrby

The structural polypeptides of two strains of measles virus grown in Vero cells were analysed in SDS-PAGE slab gels. Six major polypeptides were identified with mol. wt. of 79000, 72000, 60000, 43000, 40000 and 36000. The largest polypeptide was sensitive to trypsin digestion and was the dominant glycosylated polypeptide identified when the virus was grown in medium containing 3H-fucose or 3H-glucosamine or when the virus was treated with galactose oxidase and labelled with 3H-sodium borohydride. It is concluded that the 79000 mol. wt. polypeptide represents the haemagglutinin. Treatment with non-ionic detergent removed this polypeptide and also the 40000 mol. wt. polypeptide from the virus envelope. The 40000 mol. wt. polypeptide is probably associated with haemolysin and cell fusion activities and is analogous to the F1 of paramyxoviruses. A polypeptide of mol. wt. approx. 20000 detected after glycoprotein labelling may represent the F2 of measles virus. The 43000 mol. wt. polypeptide co-migrates with cellular actin and is the only major measles polypeptide that is heavily labelled when the virus is grown on Vero cells prelabelled with 35S-methionine. Thus it may represent cellular actin incorporated into the virus during maturation. The quantity of the 72000 mol. wt. polypeptide relative to the other major polypeptides varied considerably in different virus preparations. The role of the polypeptide could not be defined. By analogy with previously published data the 60000 and 36000 mol. wt. polypeptides are inferred to represent nucleocapsid and membrane proteins, respectively.


Virology | 1991

Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

Marion Huber; Roberto Cattaneo; Pius Spielhofer; Claes Örvell; Erling Norrby; Marius Messerli; Jean Claude Perriard; Martin Billeter

Measles virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors based on the strong cytomegalovirus enhancer-promoter and the simian virus 40 origin of replication. When expressed alone, nucleocapsid protein (N) migrates predominantly into the nucleus whereas phosphoprotein (P) is located in the cytoplasm. Coexpression of N and P proteins results in retention of the N protein in the cytoplasm, as seen also in infected cells. The retention of N protein is due to specific interactions with the P protein since coexpression of N with either the matrix or the hemagglutinin protein had no effect. Mapping of the regions of N-P interactions on P protein revealed that the carboxy-terminal 40% of P was sufficient for specific binding to N; however, the carboxy-terminal 60% of P was required for retention of N in the cytoplasm. Thus, the V and C proteins encoded within the first half of the P gene are not involved in the cytoplasmic retention of N protein. N protein might be fortuitously targeted to the nucleus as a result of its many basic amino acids, presumably destined to interact with the MV genome. However, this set of experiments has allowed to analyze in vivo the interactions between the N and P proteins.


Immunology Letters | 1991

Rapid "tea-bag" peptide synthesis using 9-fluorenylmethoxycarbonyl (Fmoc) protected amino acids applied for antigenic mapping of viral proteins.

Matti Sällberg; Ulla Rudén; Lars O. Magnius; Erling Norrby; Britta Wahren

The role of individual amino acids in binding human and macaque antibodies were determined in the human immunodeficiency virus type 1 (HIV-1) gp41, residues 594-613, and for human antibodies in the hepatitis B (HB) virus core/e antigens (HBc/eAg), residues 121-140. Decapeptides with 9 amino acids (aa) overlap were synthesised using a rapid method for simultaneous multiple peptide synthesis with 9-fluorenylmethoxycarbonyl (Fmoc) protection for the alpha-amino group of the aas. One coupling cycle including washing steps was performed within 60-90 min. The crude products were analysed by reversed-phase HPLC and PD-mass spectrometry. With the 11 decapeptides covering residues 594-613 of HIV-1 gp41, the sequences SGKLI at aa 599-603 was found to be the main recognition site for 19 human anti-HIV positive sera. Two macaques repeatedly immunized with a peptide covering aa 594-613 of gp41, preferentially recognised the sequence CTTAVPW at residues 604-610 after 1-2 months of immunisation. One macaque also recognised the sequence CSGKLI, with sera sampled greater than 10 months after start of immunisation. Out of 9 human sera from patients with chronic HB, and reactive to a peptide covering residues 121-140 of HBc/eAg, 8 were found to recognise the sequence TPPA at residues 128-131, with an individual variation within residues 125-133 in regard to N- and C-terminal ends of the recognised antigenic site. Thus, human recognition of this antigenic site overlaps the reported T- and the B-cell recognition site found in mice. We believe that this simple and rapid approach to obtain large numbers of immunologically active peptides can be useful for most laboratories interested in the immunological characterisation of proteins.


Journal of General Virology | 1987

Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B

Claes Örvell; Erling Norrby; Maurice A. Mufson

Mouse hybridomas producing antibodies against the structural proteins of strain WV4843, a subgroup B strain of respiratory syncytial (RS) virus, were produced by fusion of Sp2/0 myeloma cells with spleen cells from BALB/c mice immunized with purified preparations of the virus. After immunoprecipitation test with [35S]methionine-labelled extracellular virions, 35 clones found to produce antibodies against the fusion (F) protein, six against the member (M) protein, 21 against the nucleocapsid (NP) and eight against the phospho- (P) protein were further characterized. Immunoprecipitation with [3H]glucosamine-labelled intracellular virus polypeptides detected nine hybridoma cell lines producing antibodies against the large glyco- (G) protein of the virus. By competitive binding ELISA tests with monoclonal antibodies against each of the structural components, a minimum of two, 24, four, 15 and three epitopes were detected on the G, F, M, NP and P proteins, respectively. Eleven monoclonal antibodies directed against nine epitopes of the F protein could neutralize the infectivity of the virus. In contrast, none of the nine monoclonal antibodies against G could neutralize the infectivity of the virus. In order to find out more about the antigenic relationship between human and bovine RS virus strains all monoclonal antibodies were reacted with subgroup A RS virus and also with three different strains of bovine RS virus and one strain of caprine RS virus in immunofluorescence, ELISA and immunoprecipitation tests. In addition, 31 previously developed monoclonal antibodies against subgroup A virus were reacted with the bovine and caprine strains. The numbers of monoclonal antibodies of subgroup B specific for the B type of the two human subgroups were 9/9, 3/35, 0/6, 0/21, 0/8, for the G, F, M, NP and P proteins, respectively. No antigenic variations were found between the three bovine strains and the caprine strain. They did not react with the nine monoclonal antibodies against the G protein of subgroup B, nor did they react with nine monoclonal antibodies against subgroup A. Most but not all of the monoclonal antibodies against the other structural proteins of the two human RS virus subgroups reacted with the four strains. All 11 monoclonal antibodies against the F protein of subgroup B that could neutralize the infectivity of subgroup B also reacted with the bovine strains and neutralized their infectivity. It is concluded that although the bovine strains share many epitopes with the two human subgroups, they are antigenically distinct from the human viruses.


Virology | 1966

The relationship between the soluble antigens and the virion of adenovirus type 3. I. Morphological characteristics.

Erling Norrby

Abstract The soluble antigens of adenovirus type 3 were purified by zone centrifugation. The type-specific antigen, the hemagglutinin (HA), sedimented as a homogeneous population of particles at a rate corresponding to 50–60 S. Morphologically the HA appeared as six- or five-pointed stars with an overall diameter of 40–50 mμ. These appeared to be composed of a number of identical, tubular, capsomere-like structures, each associated with a thin club-shaped projection. The complete HA was interpreted as being formed out of 12 such capsomere-like structures arranged in accordance with icosahedral symmetry, each of them representing one facet in a pentagonal dodecahedron, and the club-shaped projections extending radially. The capsomere-like structure had an inner diameter of 20–25 A, outer diameter of 60–85 A, and was 55–80 A long, thus being somewhat smaller than the majority of free-lying capsomeres. The club-shaped projections had a length of 80–110 A and a maximum width of 40–60 A. Similar projections were found extending from the vertices of purified intact virions. The HA therefore is proposed to be a strictly symmetrical aggregate of that type of morphological subunits, which can also form the vertices of the intact virion. The particles carrying group-specific complement-fixing antigen activity had a sedimentation constant of 13 S. Their ultrastructure was identical with that of the majority of free-lying capsomeres as seen released by spontaneous disrupture of purified intact virions. The dimensions of the tubular structures were the following: inner diameter 20–30 A, outer diameter 80–90 A, and length 70–80 A.


Virology | 1983

Monoclonal antibodies against five structural components of measles virus I. Characterization of antigenic determinants on nine strains of measles virus

Hooshmand Sheshberadaran; Shou-Ni Chen; Erling Norrby

Monoclonal antibodies against five structural proteins of measles virus were used to determine the degree of antigenic variation within these proteins amongst nine strains of measles virus (four fresh wild-type isolates, two vaccine and two laboratory strains, and a strain derived from a case of subacute sclerosing panencephalitis) giving lytic infections in cell culture. The major surface proteins showed limited variations in their epitopes between the nine strains. No variations in the fusion (F) protein and only three variations in the hemagglutinin (H) protein epitopes were detected by radioimmune precipitation assay and other serological tests using a panel of 11 monoclonal antibodies against each protein. These antibody panels consisted of at least nine and six different binding groups for the H and F proteins, respectively. The two innermost proteins, the nucleocapsid and polymerase proteins, also appeared to be antigenically stable as no variation was detected between strains using in each case a panel of six hybridomas. In sharp contrast, the epitopes on the matrix (M) protein of different strains showed extensive variation in their reactivity with the nine anti-M monoclonal antibodies. The possible use of M protein epitopic markers in classification of measles virus strains is discussed.


AIDS Research and Human Retroviruses | 1987

A New Human Retrovirus Isolate of West African Origin (SBL-6669) and Its Relationship to HTLV-IV, LAV-II, and HTLV-IIIB

Jan Albert; Ulla Bredberg; Francesca Chiodi; Blenda Böttiger; Eva Maria Fenyö; Erling Norrby; Gunnel Biberfeld

A new human retrovirus of West African origin (SBL-6669) has been isolated from a patient with immunological and clinical signs of immunodeficiency. Using radioimmunoprecipitation assays (RIPA) and Western blot (WB) tests with human sera, the new virus isolate has been compared with HTLV-IV, LAV-II, and the HTLV-IIIB prototype strain of the human immunodeficiency virus (HIV). The West African isolates appeared to be members of the same virus group since their glycoproteins were antigenically indistinguishable. West African sera showed no detectable cross reaction with HTLV-IIIB glycoproteins. The external glycoprotein in the different virus strains only showed minor variations in size. The size of the transmembranous protein was not unambiguously defined. In the West African virus isolates a 30-35 kD protein was seen similar to the protein previously described possibly to represent this component. However, in SBL-6669 a distinct 41 kD protein was also identified. There were interstrain variations in the size of several viral proteins among the West African virus isolates. Only minor differences were seen between SBL-6669 and LAV-II. The variations were most pronounced in two core proteins corresponding to the 19 kD and 24 kD proteins of HTLV-IIIB. In addition, West African human retroviruses appear to differ in pathogenicity. LAV-II and SBL-6669 are associated with immunodeficiency, whereas HTLV-IV was isolated from healthy individuals. Since further spread of these viruses to other parts of the world is imminent, it is necessary to consider their antigenic and immunogenic properties in serodiagnosis of HIV infections and in planning for immunoprophylactic interventions.

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Claes Örvell

Karolinska University Hospital

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Hans Link

Karolinska Institutet

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