An immunologically active chimaeric protein containing herpes simplex virus type 1 glycoprotein D

Weis, John H.; Enquist, Lynn W.; Salstrom, John S.; Watson, Roger J.

doi:10.1038/302072a0

Cited by 60 publications

(14 citation statements)

References 18 publications

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“…The glycoprotein gD of HSV-1 has been shown to be a type-common antigen capable of inducing a host immune response which can protect against both HSV-1 and HSV-2 (10). For these reasons, the effort to produce a recombinant HSV vaccine by expression of a viral antigen in E. coli has centered on gD (44,45). The PRV gp50 has several similarities to HSV-1 gD.…”

Section: B) Discussionmentioning

confidence: 99%

Isolation, characterization, and physical mapping of a pseudorabies virus mutant containing antigenically altered gp50

Wathen¹,

Wathen²

1984

J Virol

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A pseudorabies virus variant (marl97-1) containing a mutation in a viral glycoprotein with a molecular weight of 50,000 (gp5O) was isolated by selecting for resistance to a neutralizing monoclonal antibody (MCA50-1) directed against gpSO. This mutant was completely resistant to neutralization with MCA50-1 in the presence or absence of complement, and was therefore defined as a mar (monoclonal-antibody-resistant) mutant. The mutation did not affect neutralization with polyvalent immune serum. The marl97-1 mutant synthesized and processed gp5O normally, but the mutation prevented the binding and immunoprecipitation of gpSO by MCA50-1. Thus, the mutation was within the structural portion of the gp5O gene affecting the epitope of the monoclonal antibody. The mutation was mapped by marker rescue with cloned pseudorabies restriction enzyme fragments to the short unique region of the pseudorabies genome between 0.813 and 0.832 map units. This is equivalent to a 2.1-kilobase-pair region.Pseudorabies virus (PRV) contains a double-stranded DNA genome with a molecular weight of ca. 90 x 106 (32).

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Section: B) Discussionmentioning

confidence: 99%

Isolation, characterization, and physical mapping of a pseudorabies virus mutant containing antigenically altered gp50

Wathen¹,

Wathen²

1984

J Virol

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“…It is known that herpesvirus glycoproteins are the principal antigens which induce host immune responses (Choppin & Scheid, 1980;Glorioso et al 1984;Norrild, 1980;Weis et al, 1983), and can be used as protective antigens for subunit vaccines (Ashley et al, 1985;Roberts et al, 1985). These observations encouraged us to try to prepare a vaccine for ADV.…”

Section: Protection Of Mice From Lethal Infection With Aujeszky's Dismentioning

confidence: 99%

Protection of Mice from Lethal Infection with Aujeszky's Disease Virus by Immunization with Purified gVI

Ishii

Kobayashi

Kuroki

et al. 1988

Journal of General Virology

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“…In Escherichia coli, accumulation of abnormal or defective proteins into intracellular inclusion bodies and their subsequent proteolytic degradation have been described (25). Furthermore, since the advent of recombinant DNA technology, overexpression of foreign genes in E. coli has in many instances resulted in accumulation of the gene product into inclusion bodies (13,27,33,34,36). Naturally occurring paracrystalline inclusions have also been observed in several species of Thiobacillus (26) and in Micrococcus lysodeikticus (14).…”

Section: Discussionmentioning

confidence: 99%

Protein inclusions produced by the entomopathogenic bacterium Xenorhabdus nematophilus subsp. nematophilus

Couche¹,

Gregson²

1987

J Bacteriol

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The entomopathogenic bacterium Xenorhabdus nematophilus subsp. nematophilus produces two types of intracellular inclusion bodies during in vitro culture. Large cigar-shaped inclusions (designated type 1) and smaller ovoid inclusions (designated type 2) were purified from cell lysates, using differential centrifugation in discontinuous glycerol gradients and isopycnic density gradient centrifugation in sodium diatrizoate. The inclusions, composed almost exclusively of protein, are readily soluble at high and low pH values and in the presence of cation chelators such as EDTA, anionic detergents (sodium dodecyl sulfate), or protein denaturants (urea, NaBr). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of purified inclusions revealed a single 26-kilodalton protein (IP-1) in type 1 inclusions and a 22-kilodalton protein (IP-2) in type 2 inclusions. Analysis of these proteins by isoelectric focusing in the presence of 8 M urea showed that IP-1 is acidic and IP-2 is neutral. Furthermore, each protein occurred in multiple forms differing slightly in isoelectric point. Other variations in peptides released by trypsin digestion, immunological properties, and amino acid composition revealed significant structural differences between IP-1 and IP-2. Kinetic studies using light microscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and immunoblotting procedures showed that inclusion protein synthesis occurs only during the second half of exponential culture growth. Synthesis of inclusion proteins and their aggregation to form inclusions occurred concurrently. Possible functions for these abundant proteins are discussed.Xenorhabdus species are entomopathogenic bacteria symbiotically associated with insect parasitic nematodes of the families Heterorhabditidae and Steinernematidae (1,3,30). The bacterial symbionts are asporogenous gram-negative rods, which are carried monoxenically in the intestine of nonfeeding infective-stage nematodes. On penetration of an insect host, the bacteria are released into the hemocoel. Colonization by the bacteria kills the host and establishes a suitable environment for reproduction of the nematodes by providing nutrients and inhibiting the growth of other microorganisms (1,24).When cultured in vitro, Xenorhabdus bacteria occur in two forms designated primary and secondary, which can be distinguished according to colony morphology and pigmentation on various bacteriological media, or on the basis of antibiotic production (1, 2). Both forms are pathogenic to insects, but only the primary form is isolated from infective nematodes (1). Xenorhabdus spp. will grow in a wide variety of artificial media which are rendered suitable for nematode reproduction, thus providing the basis for economical mass production of nematodes. Our nematophilus, in contrast to X. luminescens in which both primary and secondary forms produced inclusions (10). Intracellular inclusion bodies have also been described in several ultrastructural studies of Xenorhabdus spp. (4,7,15,18).In this repor...

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An immunologically active chimaeric protein containing herpes simplex virus type 1 glycoprotein D

Cited by 60 publications

References 18 publications

Isolation, characterization, and physical mapping of a pseudorabies virus mutant containing antigenically altered gp50

Isolation, characterization, and physical mapping of a pseudorabies virus mutant containing antigenically altered gp50

Protection of Mice from Lethal Infection with Aujeszky's Disease Virus by Immunization with Purified gVI

Protein inclusions produced by the entomopathogenic bacterium Xenorhabdus nematophilus subsp. nematophilus

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