Serological cross-reactivity within the picornaviruses as studied by electron microscopy

A sensitive electron microscopic method has been developed to determine the antigenic relationship within the picornavirus group. Negatively stained mixtures of antigens (poliovirus type 1 and 3, echovirus type 9, and coxsackievirus type A9) and antibodies (poliovirus type 3 and echovirus type 9 antisera) were examined under the electron microscope. The results showed clumping of homologous and heterologous viruses with both antisera, which was considered as evidence of cross-reaction. The controls showed no clumping or attachment of antibody molecules. The significance of clumping was tested by treating adenovirus type 7 with the two test antisera.

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Detection of cross-reactions by immunofluorescence within the picornavirus group

Canadian Journal of Microbiology ◽

10.1139/m70-100 ◽

1970 ◽

Vol 16 (7) ◽

pp. 601-604 ◽

Cited By ~ 3

Author(s):

R. K. Chaudhary ◽

J. C. N. Westwood

Keyword(s):

Indirect Method ◽

Fluorescent Antibody ◽

Kidney Cells ◽

Poliovirus Type ◽

Cross Reactions ◽

Antibody Staining ◽

Green Monkey ◽

Type 3 ◽

Echovirus Type

A rapid and sensitive method has been developed to determine the degree of cross-reactions within the picornavirus group by the indirect method of fluorescent antibody staining in green monkey kidney cells. The viruses included in the study were poliovirus type 1, 2, and 3; echovirus type 3, 9, and 11; and coxsackievirus type A9 and B5. It has been found that the cross-reactions are in fact extensive amongst the viruses tested. The heterologous reactions were almost as strong as homologous reactions. The degree of group reactivity was unexpected and its implication and advantages are discussed.

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The effect of cicloxolone sodium on the replication in cultured cells of adenovirus type 5, reovirus type 3, poliovirus type 1, two bunyaviruses and Semliki Forest virus

Journal of General Virology ◽

10.1099/0022-1317-73-2-407 ◽

1992 ◽

Vol 73 (2) ◽

pp. 407-411 ◽

Cited By ~ 8

Author(s):

D. J. Dargan ◽

C. B. Galt ◽

J. H. Subak-Sharpe

Keyword(s):

Semliki Forest Virus ◽

Cultured Cells ◽

Adenovirus Type ◽

Poliovirus Type ◽

Reovirus Type ◽

Type 3 ◽

Adenovirus Type 5

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THE MOLECULAR ORGANIZATION OF HUMAN ALPHA 2-MACROGLOBULIN. AN IMMUNO ELECTRON MICROSCOPIC STUDY WITH MONOCLONAL ANTIBODIES

10.1055/s-0038-1643864 ◽

1987 ◽

Author(s):

E Delain ◽

M Barrav ◽

J Tapon-Bretaudière ◽

F Pochon ◽

F Van Leuven

Keyword(s):

Monoclonal Antibodies ◽

Binding Sites ◽

Divalent Cations ◽

The Other ◽

Molecular Organization ◽

Cellular Receptor ◽

Electron Microscopic ◽

Microscopic Method ◽

Bait Region ◽

Electron Microscopic Method

Electron microscopy is a very convenient method to localize the epitopes of monoclonal antibodies (mAbs) at the surface of macromolecules for studying their tree-dimensional organization.We applied this immuno-electron microscopic method to human ct2-macroglobulin (ct2M). 29 anti-α2M mAbs have been tested with the four different forms of a2M : native and chymotrypsin-transformed tetramers, and the corresponding dimers, obtained by dissociation with divalent cations. These mAbs can be classified in three types : those which are specific for 1) the H-like transformed molecules, 2) the native molecules, and 3) those which can react with both forms of α2M.1) Among the H-like α2M specific mAbs, several react with the 20 kD-domain which is recognized by the cellular receptor of transformed a2M. This domain is located at the carboxyterminal end of each monomer. One IgG binds to the end of two adjacent tips of the H-like form.The other mAbs of this type bind to the α2M tips at non-terminal positions. Intermolecular connections built polymers of alternating α2M and IgG molecules.2) Among the native a2M-specific mAbs some are able to inhibit the protease-induced transformation of the native α2M. The binding sites of these mAbs are demonstrated on the native half-molecules. One of these mAbs was also able to react with transformed dimers, in a region corresponding very likely to an inaccessible epitope in the tetrameric transformed α2M molecule.3) Among the mAbs of this type, only two were able to inhibit the protease-induced transformation of α2M. Obviously, their epitopes should be close to the bait region of α2M. The other mAbs reacting with both α2M forms did not inhibit the α2M transformation.All these mAbs can be distinguished by the structure of the immune complexes formed with all forms of α2M. The epitopes are more easily located on the dimers and on the H-like transformed α2M than on the native molecules.From these observations, we propose a new model of the tree-dimensional organization of the human α2M in its native and transformed configurations, and of its protease-induced transformation.

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Human enterovirus infection in stray dogs. Some aspects of interest to public health

Revista do Instituto de Medicina Tropical de São Paulo ◽

10.1590/s0036-46651996000200012 ◽

1996 ◽

Vol 38 (2) ◽

pp. 157-161 ◽

Cited By ~ 3

Author(s):

Eliseu Alves Waldman ◽

Regina C. Moreira ◽

Sueli G. Saez ◽

Denise F.C. Souza ◽

Rita de C.C. Carmona ◽

...

Keyword(s):

Neutralizing Antibodies ◽

Neutralizing Antibody ◽

Human Enterovirus ◽

Poliovirus Type ◽

Stray Dogs ◽

Wild Poliovirus ◽

Antibody Titres ◽

Global Eradication ◽

Type 3 ◽

Echovirus Type

To investigate the possible role of domestic animals as reservoirs of human enteroviruses, we studied 212 stray dogs captured in different areas of the municipality of São Paulo. The captured animals were divided into 19 groups of 10 to 20 dogs each; faeces of 126 of the 212 dogs were processed for enterovirus isolation. The following viruses were isolated from 12 dogs: poliovirus type 1 (2 dogs), poliovirus type 3 (1 dog), echovirus type 7 (8 dogs) and echovirus type 15 (1 dog). Of the 12 infected animals, four had specific homotypic neutralizing antibody titres > 16. All 212 animals were tested for the presence of neutralizing antibodies to human enteroviruses. The frequency of neutralizing antibodies present in titres of > 16 was 10.3%, 3,8% and 4.3% for vaccinal prototypes of polioviruses 1, 2 and 3 respectively; 1,9%, 1.4% and 1.5% for wild prototypes of the same viruses, 11.3% for echovirus 7, and 2.4% for echovirus 15. The proportion of dogs with neutralizing antibodies varied with the virus studied. Some indication of the susceptibility of dogs to infection with human enteroviruses was demonstrated, and the importance of this fact for the Plan for Global Eradication of the Wild Poliovirus is discussed.

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