The human 90,000 heat shock protein and the Escherichia coli lon protein share an antigenic determinant

Latchman, David S.; Chan, Weng Onn; Leaver, Clare; Patel, R.; Oliver, Philip; Thangue, N B La

doi:10.1016/0305-0491(87)90419-6

Cited by 6 publications

(6 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We did not have sufficient MAb TG7A to investigate the fact that it also reacts with a heat shock-induced protein. This heat shock protein must express a similar epitope (Latchman et al, 1987) and this accounts for the results obtained by Latchman & La Thangue (1988). We have not detected these proteins immunologically in our rat cells (RE, Bn5T or rat 1 cells) (Macnab et al, 1985).…”

supporting

confidence: 48%

“…Although TBS, antisera raised to HSV-infected cells and MAb TG7A all recognize a similar U90 and L90 in Bn5T cells by immunoprecipitation, it is clear that in denatured proteins MAb TG7A recognizes an epitope different to those recognized by the polyclonal antisera. Evidence of this is provided by the observation that MAb TG7A recognizes an epitope on the Escherichia coli Ion protease (Latchman et al, 1987) and reacts generally with E. coli antigens. Neither TBS nor the antisera raised against HSV-2-infected cells react with E. coil proteins, as determined by screening cDNA libraries (D. McNab & J. C. M. Macnab, unpublished results).…”

mentioning

confidence: 99%

See 1 more Smart Citation

A Transformation-specific Polypeptide Distinct from Heat Shock Proteins is Induced by Herpes Simplex Virus Type 2 Infection

Hewitt

Grassie

McNab

et al. 1991

Journal of General Virology

View full text Add to dashboard Cite

A tumour-specific polypeptide designated U90 is one of a set of polypeptides which are encoded by the host cell and are specific for the transformed cell state, being immunoprecipitated by the sera of tumour-bearing animals. The interest in these tumour-specific polypeptides centres on the finding that they are also recognized by antisera raised against herpes simplex virus type 2 (HSV-2)-infected cells, implying some role for HSV-2 in tumorigenesis. The peptide map of HSV-2-induced U90 is indistinguishable from that of U90 present in uninfected tumour cells, including mouse cells transformed by human papillomavirus type 16. In tumour cells, U90 is located principally in the plasma membrane fraction and cannot be induced by heat shock, glucose starvation, or treatment with tunicamycin or calcium ionophore. U90 is not related to either the heat shock protein of Mr 90000 (HSP90) or the glucose-related polypeptide of Mr 94000 (GRP94) as determined by peptide mapping and the use of monospecific, monoclonal and antipeptide antibodies. This suggests that U90 is a novel transformationspecific protein which can be induced by infection with HSV-2.Macnab et al. (1985) have shown that a specific set of polypeptides of Mr 90000 (a doublet), 40000 and 32000 are immunoprecipitated from transformed cells by antisera (TBS) from tumour-bearing animals or sera raised against cells infected with herpes simplex virus type 2 (HSV-2) strain HG52, or by a mouse monoclonal antibody (MAb), TG7A. This polypeptide set could not be immunoprecipitated from control embryo cells.In this study we have characterized the 90000 Mr polypeptide doublet identified by immunoprecipitation, described its localization in the cell, and demonstrated that it is not induced by heat shock and does not possess any similarity to stress proteins such as heat shock protein, HSP90 (Mr 90000), or the glucose-regulated polypeptide, GRP94 (Mr 94000). In addition, it is shown that infection of transformed Bn5T cells with HSV-2 (HG52) increases the amount of the upper polypeptide band (U90) of the 90K doublet by 2.5-to fivefold, whereas the amount of the lower polypeptide band (L90) does not increase.For these experiments we employed rat embryo (RE) cells as control cells and Bn5T cells (a cell line derived from a tumour induced by transformation of RE cells with the BgllI n fragment of HSV-2) as transformed cells, and the assay used to derive the results was immunoprecipitation of L-[ 35S]methionine_labelled polypeptides (Macnab et al., 1985). The immunoprecipitates were trapped using Protein A-Sepharose (Sigma) or 0001-0270 © 1991 SGM Pansorbin (Calbiochem), and the radiolabelled proteins were visualized by autoradiography after separation by electrophoresis on 7 or 7.5% polyacrylamide gels. Polypeptide extractions were carried out in RIPA buffer (Macnab et al., 1985) containing three protease inhibitors, 0.034 mg/ml PMSF, 0-03 mg/ml benzamidine and 0.1 mg/ml phenanthroline.Polyclonal antisera were raised in mice against HSV-2 (HG52)-infected BHK C13 cells and in r...

show abstract

supporting

confidence: 48%

mentioning

confidence: 99%

A Transformation-specific Polypeptide Distinct from Heat Shock Proteins is Induced by Herpes Simplex Virus Type 2 Infection

Hewitt

Grassie

McNab

et al. 1991

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…Numerous genera of bacteria produce structurally related heat shock proteins, demonstrating a high degree of evolutionary conservation (221). A human heat shock protein and the Lon protein of E. coli share at least one antigenic determinant (138). Besides the evolutionary implications and the molecular mimicry involved in this relationship, the heat shock phenomenon may have additional importance.…”

Section: Concluding Thoughtsmentioning

confidence: 99%

Contemporary issues: diseases with a food vector

1988

View full text Add to dashboard Cite

Foodborne disease has become a contemporary issue. Several large, well-publicized outbreaks of foodborne disease have heightened public awareness that harmful microorganisms may be present in food and that chronic as well as acute disease may be caused by foodborne microbes. The field of food microbiology has likewise experienced a resurgence of interest. New tools, such as recombinant deoxyribonucleic acid technology and monoclonal antibody production, used to elucidate microbial virulence factors have facilitated identification of disease-causing microbes once thought to be harmless and demonstrated the complexity of individual virulence mechanisms previously considered to be well understood. Foodborne pathogens are also causing disease via some surprising food vectors, such as chopped, bottled garlic and sauteed onions. In addition to acute gastrointestinal disturbances, certain microorganisms may, through complex interactions with the human immune response, cause chronic diseases that affect several major organ systems. These microbes are serving as models in studies of molecular mimicry and genetic interrelatedness of procaryotes and eucaryotes. Other recently recognized attributes of foodborne microorganisms, such as the heat shock phenomenon and the possible nonculturability of some bacteria, may affect their ability to cause disease in humans. Because foodborne disease is a major cause of morbidity and mortality, the study of these diseases and their causative microorganisms presents a unique challenge to many professionals in the subdisciplines of microbiology, epidemiology, and clinical medicine.

show abstract

“…Such a possibility is supported by the finding that HSV infection does not induce acaumulation of the 650 bp ubiquitin n8ZN species which has been shown in both human and rat to encode a nuclear form of ubiquitin that is stably conjugated to histone H2A and is not involved in proteolytic degradation (23,42). It is likely therefore that the induction of ubiquitin in HSV infection represents one aspect of a co-ordinate induction of cellular &grtive patbways which also results in the accumulaticr of a protein hamlogous to the L<n protease of E.coli, a protein which is involved in the dgadation of abnormal or denatured proteins (43,44,45). Although in cultured cells, such attexpts to inhibit the prors of the viral lytic cycle are usually unsuccessful, it is possible that during infection of sane cell types in vivo, they may cause the lytic cycle to be abrted, resulting in either latent infection (46) or possibly cellular transfonmticn (47) by HSV.…”

Section: Discijssicnmentioning

confidence: 99%

Transcriptional induction of the ubiquitin gene during herpes simplex virus infection is dependent upon the viral immediate-early protein ICP4

1987

Self Cite

View full text Add to dashboard Cite

Lytic infection with herpes simplex virus results in transcriptional induction of a cellular gene encoding ubiquitin, causing increased accumulation of ubiquitin RNA and protein in the infected cell. This induction, which is dependent upon viral protein synthesis, does not occur in the HSV-1 mutant tsK which is defective in the gene encoding the viral protein ICP4. Transfected cells expressing the viral ICP4 protein exhibit higher levels of ubiquitin gene transcription than untransfected controls indicating that transcriptional induction can be mediated by the ICP4 protein alone.

show abstract

The human 90,000 heat shock protein and the Escherichia coli lon protein share an antigenic determinant

Cited by 6 publications

References 21 publications

A Transformation-specific Polypeptide Distinct from Heat Shock Proteins is Induced by Herpes Simplex Virus Type 2 Infection

A Transformation-specific Polypeptide Distinct from Heat Shock Proteins is Induced by Herpes Simplex Virus Type 2 Infection

Contemporary issues: diseases with a food vector

Transcriptional induction of the ubiquitin gene during herpes simplex virus infection is dependent upon the viral immediate-early protein ICP4

Contact Info

Product

Resources

About