| 1. |
- Johansson, Hugo, et al.
(författare)
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Human immunoglobulin class and subclass specificity of Fc receptors induced by herpes simplex virus type 1
- 1984
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Ingår i: Journal of Virology. - 1098-5514. ; 50:3, s. 796-804
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Tidskriftsartikel (refereegranskat)abstract
- Herpes simplex virus is known to induce an immunoglobulin-binding cell surface receptor in infected cells that utilizes a nonimmune mechanism. In the present paper, we report the immunoglobulin class and subclass specificity of this receptor. Of the human immunoglobulins G(IgG), IgA, IgM, and IgD, as well as the structurally related beta2 microglobulin, only IgG and its Fc portion exhibited an increased binding to herpes simplex virus-infected cells versus uninfected control cells. The IgG subclass specificity of the Fc receptor was studied in 37 radioiodinated IgG myeloma proteins representing all four subclasses. We found that IgG3 myeloma proteins did not bind to herpes simplex virus-infected cells to a greater extent than to uninfected cells. On the contrary, proteins belonging to the other subclasses exhibited an increased binding to herpes simplex virus-infected cells of the following relative magnitude: IgG4 greater than IgG1 greater than or equal to IgG2. This increment of binding could be abolished by addition of a large excess of human IgG Fc fragment. Evidence for the existence of a variable herpes simplex virus-specific binding ability between myeloma proteins belonging to the same IgG subclass was also obtained. Furthermore, we tested two other herpes simplex virus type 1 strains with a limited number of myeloma proteins with very similar results as with the herpes simplex virus type 1 F strain. Several sources of experimental artefacts were controlled, including the state of aggregation of the test proteins, the functional integrity of the Fc portion before and after radioiodination, and the subclass assignments. The implications for the biological role of the Fc receptor of herpes simplex virus are discussed.
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| 2. |
- Johansson, Hugo, et al.
(författare)
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Specificity of Fc receptors induced by herpes simplex virus type 1: comparison of immunoglobulin G from different animal species
- 1985
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Ingår i: Journal of Virology. - 1098-5514. ; 56:2, s. 489-494
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Tidskriftsartikel (refereegranskat)abstract
- Cells infected with herpes simplex virus type 1 (HSV-1) express a cell surface receptor able to bind the Fc portion of immunoglobulin G (IgG). Of the four human IgG subclasses, the HSV-1 Fc receptor, like staphylococcal protein A, binds to all except IgG3. In this paper, we describe the binding of a number of animal IgG and IgG subclass molecules to HSV-1-infected cells and compare this binding to that of protein A. Although only few representatives from each animal order were tested, we found that IgG from Carnivora and Rodentia did not bind or bound only slightly to the HSV-1 receptor, whereas IgG from Primates, Lagomorpha, and Artiodactyla bound well. This pattern was clearly different from the species spectrum of IgG binding of protein A. Differences between the two receptors were also found when animal IgG subclasses were tested. The pronounced differences in affinity for the HSV-1 Fc receptor between immunoglobulins from, for example, mouse and rabbit may influence the interpretation of animal studies with this virus.
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| 3. |
- Stålhanske, P.O.K., et al.
(författare)
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Replicase Gene of Coxsackievirus B3
- 1984
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Ingår i: Journal of Virology. - 0022-538X .- 1098-5514. ; 51:3, s. 742-746
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Tidskriftsartikel (refereegranskat)abstract
- A cDNA copy covering two-thirds of the coxsackievirus B3 genomewas cloned in the PstI site of the pBR322 vector. A nucleotidesequence containing the gene for the viral replicase and the3' noncoding region of the coxsackievirus B3 genome was determined.The predicted amino acid sequence of the coxsackievirus B3 replicasewas shown to be remarkably similar to that of the poliovirus1 replicase. The 3' noncoding region, in contrast, was onlyweakly homologous to the poliovirus 1 sequence but showed aclose relationship to the sequence of swine vesicular diseasevirus, a variant of coxsackievirus B5. A 13-nucleotide-longsegment located near the polyadenylic acid junction is conservedin several members of the enterovirus group and may thus servean important function during replication of viral RNA.
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