Antibodies to human cytomegalovirus structural polypeptides during primary infection

Landini, Maria Paola; Rossier, E; Schmitz, Herbert

doi:10.1016/0166-0934(88)90113-9

Cited by 49 publications

(35 citation statements)

References 17 publications

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“…HCMV ppUL83 appears to be one of the most immunogenic structural antigens of HCMV (Schmidt et al, 1980;Pereira et al, 1982aPereira et al, , 1983Lery et al, 1982;Cremer et al, 1985;Landini et al, 1985Landini et al, , 1986Jahn et al, 1987b). The ppUL83-specific antibody response is very high during the acute phase of infection, as well as during early convalescence, but decreases thereafter (Pereira et al, 1982b(Pereira et al, , 1983Forman et al, 1985;Landini et al, 1985Landini et al, , 1986Jahn et al, 1987b;Porath et al, 1987;Gold et al, 1988;Landini et al, 1988b). A study aimed at analysing the appearance of serum IgG and IgM against HCMV structural proteins in sequential sera from renal transplant recipients during the first 1 to 3 months of primary infection has shown that very often the first antibodies to appear are specific for ppUL83 .…”

Section: (Iii) Pp Ul82 and (Iv) Pp Ul83mentioning

confidence: 99%

Human cytomegalovirus structural proteins

Spaete¹,

Gehrz²,

Landini³

1994

Journal of General Virology

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Section: (Iii) Pp Ul82 and (Iv) Pp Ul83mentioning

confidence: 99%

Human cytomegalovirus structural proteins

Spaete¹,

Gehrz²,

Landini³

1994

Journal of General Virology

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“…Several studies have investigated antibody specificities against structural proteins of HCMV in detail (21,22,23,24). Proteins which could correspond to gpTRL10 were not well described.…”

Section: Discussionmentioning

confidence: 99%

Identification of Glycoprotein gpTRL10 as a Structural Component of Human Cytomegalovirus

Spaderna

Blessing

Bogner

et al. 2002

J Virol

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Human cytomegalovirus (HCMV) has a coding capacity for glycoproteins which far exceeds that of other herpesviruses. Few of these proteins have been characterized. We have investigated the gene product(s) of reading frame 10, which is present in both the internal and terminal repeat regions of HCMV strain AD169 and only once in clinical isolates. The putative protein product is a 171-amino-acid glycoprotein with a theoretical mass of 20.5 kDa. We characterized the protein encoded by this reading frame in the laboratory strain AD169 and a recent isolate, TB40E. The results from both strains were comparable. Northern blot analyses showed that the gene was transcribed with early/late kinetics. Two proteins of 22 and 23.5-kDa were detected in virus-infected cells and in cells transiently expressing recombinant TRL10. Both forms contained only high-mannose-linked carbohydrate modifications. In addition, virus-infected cells expressed small amounts of the protein modified with complex N-linked sugars. Image analysis localized transiently expressed TRL10 to the endoplasmic reticulum. Immunoblot analyses as well as immunoelectron microscopy of purified virions demonstrated that TRL10 represents a structural component of the virus particle. Immunoblot analysis in the absence of reducing agents indicated that TRL10, like the other HCMV envelope glycoproteins, is present in a disulfide-linked complex. Sequence analysis of the TRL10 coding region in nine low-passage clinical isolates revealed strain-specific variation. In summary, the protein product of the TRL10 open reading frame represents a novel structural glycoprotein of HCMV and was termed gpTRL10.

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“…Study Population Serial serum specimens were obtained from 24 patients (median age 37 yr, range 23 to 60; 16 males) undergoing solid organ transplantation (22 kidney, 2 heart) from 1986 through 1989. These sera were collected during prospective surveillance for CMV infection in transplant patients at the University of Ottawa; data from this program have been published before [Landini et al, 1988;Miller et al, 19911. All patients were monitored by viral culture and serology at approximately monthly intervals.…”

Section: Methodsmentioning

confidence: 99%

Ontogeny of glycoprotein gB‐specific antibody and neutralizing activity during natural cytomegalovirus infection

Marshall

Stout

Knights

et al. 1994

Journal of Medical Virology

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The envelope glycoprotein gB (gpUL55) is a candidate for inclusion in subunit cytomegalovirus (CMV) vaccines, although data on gB antibody responses after natural infection are limited. [35S]-labeled gB was partially purified from cells infected with an adenovirus recombinant expressing gB and used in radioimmunoprecipitation assays to characterize responses in solid organ transplant recipients with primary (n = 11) or secondary (n = 8) CMV infection. Seropositive transplant patients without evidence of infection (n = 5) and healthy seroconverters (n = 7) were also studied. gB antibody developed concurrently with CMV-specific IgG, IgM, and neutralizing activity in transplant patients with primary infection. Sustained boosts in gB antibody were seen in patients with secondary infection, and healthy seroconverters developed early gB responses. These data imply that gB antibody is an integral part of the humoral response to CMV infection, and, in view of experimental data regarding immunogenicity, support a role for gB in subunit vaccines.

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Antibodies to human cytomegalovirus structural polypeptides during primary infection

Cited by 49 publications

References 17 publications

Human cytomegalovirus structural proteins

Human cytomegalovirus structural proteins

Identification of Glycoprotein gpTRL10 as a Structural Component of Human Cytomegalovirus

Ontogeny of glycoprotein gB‐specific antibody and neutralizing activity during natural cytomegalovirus infection

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