Bad consequences of bicycle accidents. Pyomyositis.
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Accidents, Traffic↗
Biomedical subjects
C Grose
Publications and source records attributed to C Grose.
Congenital infections caused by varicella zoster virus and herpes simplex virus.
Congenital infections are caused by both varicella-zoster virus (VZV) and herpes simplex virus type 2 (HSV-2). The VZV fetopathy and the HSV fetopathy exhibit several similarities. Both affect the skin, eyes and brain, often with devastating consequences. Congenital VZV infection also may damage portions of the cervical or lumbosacral plexi, an insult that leads to denervation and maldevelopment of an extremity. As is evident from the pathology, most of the fetal sequelae caused by intrauterine infection with VZV and HSV-2 are caused by the pronounced neurotropism of both alpha-herpes viruses.
Chickenpox↗
Entry and egress of varicella virus blocked by same anti-gH monoclonal antibody.
Varicella virus is one of the most reclusive human herpesviruses. The virus is not released from infected cultured cells. Rather, infectivity is transferred by fusion of contiguous cells. To further investigate this process, infected cells were viewed by scanning electron microscopy. Thousands of viral particles were observed in elongated clusters overlying the virus-induced syncytia. When virus-infected cells were covered postinfection with medium supplemented with a monoclonal antibody to glycoprotein gpIII (gH homolog), syncytial formation was completely blocked and no progeny viral particles were observed on the surface of the monolayer. Removal of the antibody was followed by rapid progression of cytopathic effect. Addition of antibody to other viral proteins did not alter the infection. Thus, a monoclonal antibody to a single viral determinant on glycoprotein gpIII (gH) can prevent syncytial formation postinfection and block progression of infectivity. Since the same monoclonal antibody can inhibit entry, this study greatly expands the role of antibody in the modulation of herpesvirus infection.
Antibodies, Monoclonal↗
Magnetic resonance imaging for early diagnosis of necrotizing fasciitis.
One of the most serious complications of chickenpox is varicella gangrenosa, a form of necrotizing fasciitis. A confounding factor is the frequency of more superficial skin infections during chickenpox, often caused by group A beta-hemolytic streptococcus. Because the progression from cellulitis to fasciitis is so insidious, severe tissue necrosis often has occurred before the correct diagnosis is made on the basis of clinical examination. Even today, limb amputation is occasionally required for treatment of gangrenous varicella. In this report, we demonstrate that magnetic resonance imaging can delineate the degree and depth of inflammation within an extremity and, thereby, indicate when the infection is progressing despite antibiotic therapy. Thus, the earlier use of magnetic resonance imaging may facilitate the diagnosis of necrotizing fasciitis.
Chickenpox↗
Varicella-zoster virus glycoprotein gpI/gpIV receptor: expression, complex formation, and antigenicity within the vaccinia virus-T7 RNA polymerase transfection system.
The unique short region of the varicella-zoster virus (VZV) genome contains two open reading frames which encode glycoproteins designated gpI and gpIV (herpes simplex virus homologs gE and gI, respectively). Like its herpesviral counterpart gE, the VZV gpI gene product functions as a cell surface receptor (V. Litwin, W. Jackson, and C. Grose, J. Virol. 66:3643-3651, 1992). To evaluate the biosynthesis of the two VZV glycoproteins and further explore their relationship to one another, the two glycoprotein genes were individually cloned into a pTM1 vector under control of the T7 promoter. Transfection of the cloned gpI or gpIV construct into HeLa cells previously infected with vaccinia recombinant virus expressing bacteriophage T7 polymerase resulted in a much higher level expression of each VZV glycoprotein than previously achieved. Synthesis of both gpI and gpIV included intermediary partially glycosylated forms and mature N- and O-linked final product. Transfections in the presence of 32Pi demonstrated that the mature forms of both gpI and gpIV were phosphorylated, while similar experiments with [35S]sulfate showed that only the mature gpI was sulfated. When gpI and gpIV were coexpressed in the same cell, the two glycoproteins were complexed to each other, as both proteins could be immunoprecipitated by antibodies against either gpI or gpIV. Coprecipitation did not occur as a result of a shared epitope, because gpI expressed alone was not precipitated by antibody to gpIV, and gpIV expressed alone was not precipitated by antibody to gpI. Pulse-chase analysis demonstrated that the gpI-gpIV association occurred early in processing; furthermore, this complex formation interfered with posttranslational modifications and thereby reduced the M(r)s of the mature forms of both gpI and gpIV. Similarly, the molecular masses of the cotransfected gene products corresponded with those of the infected cell glycoproteins, a result which suggested that authentic gpI and gpIV were ordinarily found within a complex. Thus, the adjacent open reading frames 67 and 68 code for two glycoproteins which in turn form a distinctive sulfated and phosphorylated cell surface complex with receptor properties.
Antibodies, Monoclonal↗
Identification of the phosphorylation sequence in the cytoplasmic tail of the varicella-zoster virus Fc receptor glycoprotein gpI.
Varicella-zoster virus (VZV) glycoprotein gpI, the homolog of herpes simplex virus gE, functions as a receptor for the Fc portion of immunoglobulin G. Like other cell surface receptors, this viral receptor is highly phosphorylated in cell culture. To identify the precise location of the cellular kinase-mediated phosphorylation, we generated a tailless deletion mutant and several point mutants which had altered serine and threonine residues within the cytoplasmic domain of gpI. The mutated and wild-type genes of gpI were transfected and expressed within a vaccinia virus-T7 polymerase transfection system in order to determine what effect these mutations had on the phosphorylation state of the protein in vivo and in vitro. Truncation of the cytoplasmic domain of gpI diminished the phosphorylation of gpI in vivo. Examination of the point mutants established that the major phosphorylation sequence of gpI was located between amino acids 593 and 598, a site which included four phosphorylatable serine and threonine residues. Phosphorylation analyses of the mutant and wild-type glycoproteins confirmed that gpI was a substrate for casein kinase II, with threonines 596 and 598 being critical residues. Although the mutant glycoproteins were phosphorylated by casein kinase I, protease V8 partial digestion profiles suggested that casein kinase II exerted the major effect. Thus, these mutagenesis studies demonstrated that the gpI cytoplasmic sequence Ser-Glu-Ser-Thr-Asp-Thr was phosphorylated in mammalian cells in the absence of any other herpesvirus products. Since the region defined by transfection was consistent with results obtained with in vitro phosphorylation by casein kinase II, we propose that VZV gpI is a physiologic substrate for casein kinase II. Immunofluorescence and pulse-chase experiments demonstrated that the mutant glycoproteins were processed and transported to the outer cell membrane.
Amino Acid Sequence↗
Herpesvirus antibody levels in the etiologic diagnosis of the acute retinal necrosis syndrome.
Quantitative antibody levels to three herpesviruses in acute and chronic sera from six patients with clinical signs of the acute retinal necrosis syndrome were consistent with a specific etiologic diagnosis only in the two cases associated with cutaneous herpes zoster. Available data on acute and convalescent antibody titers to herpes group viruses from these six patients in addition to data from 27 acute retinal necrosis cases from the literature disclosed that only 13 of the 33 patients (39%) had a diagnostic increase or decrease in herpes group viral antibody levels on serial sampling. Three patients had nondiagnostic changes in viral antibody levels despite positive vitreous cultures for herpesviruses. In contrast, a review of 25 cases from the literature with paired antiviral serum and intraocular fluid antibody levels suggested a more promising approach to the etiologic diagnosis of the acute retinal necrosis syndrome. By calculating the ratio of antiviral antibodies in intraocular fluid and serum, an etiologic diagnosis could be made in 12 of 14 (86%) of subacute and convalescent samples. The sensitivity of this method decreased to 72% (13 of 18) when fluids were obtained earlier in the course of the disease.
Adult↗
Herpesviral Fc receptors and their relationship to the human Fc receptors.
Nearly two decades ago, it was observed that cells infected with herpes simplex virus (HSV) acquired an IgG Fc binding activity. The properties of the viral Fc receptor (FcR) have now been characterized by several laboratories. The Fc binding activity appears on the surface of the infected cell prior to formation of progeny virions. The FcR induced by HSV has been identified as the HSV glycoprotein, gE. When HSV gE forms a complex with a second HSV glycoprotein, gI, the receptor binds IgG with higher affinity. Varicella-zoster virus (VZV), which is closely related to HSV, has also been shown to induce an FcR. Like the HSV FcR, the FcR specified by VZV possesses characteristics common to viral glycoproteins. VZV encodes two glycoproteins, gpI and gpIV, which are the homologs of HSV gE and gI. The VZV glycoproteins have many properties common to cell surface receptors, including O-linked glycans and phosphorylation sites. However, extensive computer-assisted analyses of the amino acid sequences of VZV gpI and gpIV did not uncover regions of homology to the human cellular Fc receptors for IgG.
Amino Acid Sequence↗
Serine protein kinase associated with varicella-zoster virus ORF 47.
Varicella-zoster virus (VZV) ORF 47 lies in the unique long region of the VZV genome. Sequence homology studies have demonstrated that gene 47 possessed conserved protein kinase motifs. In this study, we investigated the properties of the ORF 47 product. First, a rabbit antiserum was raised against a protein generated from the fusion of the most antigenic ORF 47 domain with Escherichia coli beta-galactosidase. The high-titer antiserum reacted specifically with ORF 47 polypeptides translated in vitro. When incubated with VZV-infected cell lysate, the antiserum immunoprecipitated a phosphoprotein of M(r) 54,000, a size comparable with the predicted molecular mass. The precipitated viral protein was phosphorylated in a protein kinase assay; subsequent phosphoamino acid analysis indicated that the phosphotransferase associated with the ORF 47 protein was a serine protein kinase. Synthesis of the ORF 47 product in VZV-infected cell culture increased in the first and second days and plateaued after the third day of infection. The protein kinase activity associated with VZV ORF 47 had several distinctive biochemical properties: (i) its phosphotransferase activity was enhanced more by manganese than by magnesium, (ii) it utilized both ATP and GTP as donors of phosphate, and (iii) it phosphorylated both acidic and basic substrates. In summary, this report lends support to the computer homology data which predicted that VZV ORF 47 would encode a serine protein kinase.
Antibodies, Viral↗
Intracellular synthesis of varicella-zoster virus.
Varicella-zoster virus, a reclusive alpha-herpesvirus, can be isolated and propagated in a limited number of human cell lines. Under in vitro conditions, the virus is strongly cell-associated and, therefore, difficult to recover in a truly cell-free state. The general replication cycle includes the three phases called immediate early, early, and late. An example of an early viral protein is a putative protein kinase called open reading frame (ORF) 47. An example of a late protein is the preponderant viral glycoprotein (ORF 68) designated VZV gpI.
Amino Acid Sequence↗
Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction.
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Base Sequence↗
Receptor properties of two varicella-zoster virus glycoproteins, gpI and gpIV, homologous to herpes simplex virus gE and gI.
The varicella-zoster virus (VZV) genome contains 70 reading frames (ORF), 5 of which encode the glycoproteins gpI, gpII, gpIII, gpIV, and gpV. ORF 67 and 68 lie adjacent to each other in the unique short region of the VZV genome and code for gpIV and gpI, respectively. These two genes, which are contained within the HindIII C fragment of the VZV genome, were subcloned in the correct orientation downstream from the promoter regions of the eukaryotic expression vectors pCMV5 and pBJ. After transfection, 5 to 20% of the Cos cells bound antibody specific for the given glycoprotein. In this study, it was shown that only the cells transfected with the gpI construct bound to the Fc fragment of human immunoglobulin G. Neither the transfected gpIV gene product nor the vector only bound to the Fc fragment. Thus, VZV gpI is confirmed to be the VZV-encoded Fc-binding glycoprotein. Like the wild-type form of gpI expressed in VZV-infected cells, gpI precipitated from transfected cells contained both N-linked and O-linked glycans and was heavily sialated. In addition, the transfected gpI gene product was phosphorylated both in cell culture and in protein kinase assays by mammalian casein kinases I and II. Extensive computer-assisted analyses of the VZV gpI sequence, as well as those of alphaherpesviral homolog glycoproteins, disclosed properties similar to those of other cell surface receptors; these included (i) exocytoplasmic regions rich in cysteine residues, (ii) membrane-proximal regions with potential O-linked glycosylation sites, and (iii) cytoplasmic domains with consensus phosphorylation sites.
Amino Acid Sequence↗
Prenatal diagnosis of congenital cytomegalovirus infection by virus isolation after amniocentesis.
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Amniocentesis↗
Fatal pertussis in an Iowa infant.
Much media attention has been paid to neurological disease induced by DPT vaccine, but what about the risk of pertussis to unimmunized children? The authors present a case report of fatal whooping cough in a 5-week-old baby.
Diagnosis, Differential↗
Prenatal diagnosis of congenital cytomegalovirus infection by virus isolation from amniotic fluid.
Cytomegalovirus was isolated antenatally from the amniotic fluid of two pregnant women. In both cases prenatal diagnosis of the fetal virus infection aided the subsequent management of the mother and newborn infant.
Adolescent↗
Prenatal diagnosis of congenital cytomegalovirus infection: two decades later.
Cytomegalovirus is the most common cause of congenital infection in the United States, yet there has been little progress in the prenatal diagnosis of this intrauterine infection. We present evidence that viral culture of amniotic fluid may be a useful adjunct procedure, when performed as part of the antenatal evaluation of suspected fetal cytomegalovirus infection.
Amniocentesis↗
Cell surface expression of the varicella-zoster virus glycoproteins and Fc receptor.
Varicella-zoster virus (VZV) specifies the synthesis of viral glycoproteins which are important antigens for induction of the host immune response. In this report the technology of laser-activated flow cytometry has been employed to measure the membrane expression of VZV glycoproteins gpI, gpII, gpIII, and gpIV. By use of biotinylated monoclonal antibodies as probes, all four glycoproteins were demonstrated on the infected cell surface. The temporal appearance of the viral glycoproteins was defined in a time course experiment and shown to be maximal about 24 hr postinfection. The issue whether VZV induces the cell surface expression of an Fc receptor (FcR) was investigated with biotinylated nonimmune human IgG, followed by streptavidin-phycoerythrin. By this technique a 10-fold increase in fluorescence intensity was seen in the VZV-infected cells as compared to the mock-infected controls. When the experiment was repeated with purified human Fc fragment rather than whole IgG, a similar degree of binding was seen. Both the VZV glycoproteins and the VZV FcR were exquisitely sensitive to trypsin treatment (1 mg/ml); likewise, the cell surface expression of these VZV products was diminished by treatment of the infected cultures with monensin, an inhibitor of glycoprotein transport. In order to prove that VZV infection was not causing the induction of a cellular Fc gamma R, the VZV-infected and mock-infected cells were stained with monoclonal antibodies directed against each of the three human cellular IgG FcR, but no differences were observed. Therefore, the FcR activity seen in the infected culture was not due to one of the known cellular Fc gamma R.
Antigens, Viral↗
Glycoproteins encoded by varicella-zoster virus: biosynthesis, phosphorylation, and intracellular trafficking.
This article reviews major developments concerning the VZV glycoproteins. Very little was published about these viral products prior to the early 1980s. VZV is now known to encode five glycoproteins that have been designated gpI through gpV. The viral glycoproteins are present within the envelope of the complete virion; in addition, they are inserted in the plasma membrane of the infected cell. Studies of the assembly and processing of three of the VZV glycoproteins have demonstrated that they may contain both N-linked and O-linked glycans, some of which are also sulfated and sialated. A heretofore unappreciated modification of VZV gpI is phosphorylation. The glycoprotein is modified on its serine and threonine residues by at least two cellular protein kinases--casein kinases I and II. Finally, aspects of viral glycoprotein trafficking have been analyzed in VZV-infected cells. The pathway progresses from the trans-Golgi region via cytoplasmic vacuoles to the outer cellular membrane. The virus may acquire part of its glycoprotein-laden envelope from the cytoplasmic vacuoles.
Glycoproteins↗