Maternity services: the shaping of things to come.
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Clinical Competence↗
Biomedical subjects
L Dillner
Publications and source records attributed to L Dillner.
Antigenic and immunogenic epitopes shared by human papillomavirus type 16 and bovine, canine, and avian papillomaviruses.
All types of papillomaviruses (PV) share common, so-called group-specific epitopes. To identify the major group-specific epitopes, we immunized 26 guinea pigs or rabbits with purified bovine PV type 1 (BPV), canine PV, or avian PV from the common chaffinch. The resulting hyperimmune sera, as well as a commercially available rabbit antiserum to BPV and seven monoclonal antibodies to BPV, were tested in an enzyme-linked immunosorbent assay with a set of 66 overlapping 20-amino-acid peptides representing the complete sequence of the major capsid proteins (L1 and L2) of human PV type 16 (HPV 16). Sera from the same animals before immunization were used as controls. The minimal reactive epitopes within each peptide were further characterized by testing of truncated peptides. The cross-reactive epitopes were clustered in two regions of L1, an internal region (at positions 171 to 235), which contained three epitopes, and the more reactive region at the carboxy terminus (at positions 411 to 475), which contained six epitopes. The most reactive of the HPV 16 broadly cross-reactive epitopes was a carboxy-terminal epitope which had the sequence DTYRF and which reacted with nine of the antisera to BPV, canine PV, or avian PV, with the commercially available rabbit antiserum to BPV, and also with a mouse monoclonal antibody to BPV. Antipeptide antisera to all of the HPV 16 L1 peptides and to the most antigenically reactive of their truncated analogs were made in guinea pigs. Antipeptide antisera reactive with BPV were obtained for three of the cross-reactive epitopes, and one of these antisera allowed highly sensitive detection of group-specific PV antigen by immunoperoxidase staining.
Amino Acid Sequence↗
Mapping of linear epitopes of human papillomavirus type 16: the L1 and L2 open reading frames.
Certain types of human papillomavirus (HPV), notably HPV type 16, are associated with flat or inverted proliferative lesions of the cervix uteri that can progress to malignancy. As a first step towards the serological study of the epidemiology of HPV, we have synthesized the entire amino acid sequences of the 2 major viral capsid proteins of HPV type 16, L1 and L2, as a set of 66 synthetic 20-residue peptides with an overlap of 5 amino acids. The peptides were tested for reactivity with IgA, IgG and IgM antibodies in the sera of 30 patients with HPV-16-carrying cervical neoplasms. Both IgG and IgM antibody responses were detected, but most of the reactivity found was of the IgA class. The most immunoreactive peptides were further analyzed for reactivity with sera from 22 patients with parotid gland tumors and with sera from 38 healthy individuals. The L2-encoded protein contained only one major linear epitope, which was not specific for HPV-16-carrying neoplasms. In contrast, the L1-encoded protein contained several epitopes that were regularly immunoreactive with antibodies present in the sera of patients with HPV-16-carrying cervical neoplasms, but only rarely so in the sera of patients with other tumors or of healthy individuals.
Amino Acid Sequence↗
Serological responses to papillomavirus group-specific antigens in women with neoplasia of the cervix uteri.
Certain types of human papillomaviruses have been linked to the development of carcinoma of the cervix uteri. We have analyzed 114 serum specimens from women with cervical intraepithelial neoplasia (CIN) or carcinoma of the cervix uteri for the presence of serum antibodies against purified, disrupted bovine papillomavirus (BPV). The titers of immunoglobulin A (IgA) antibodies against BPV were slightly elevated (P less than 0.025) in the sera from CIN or cervical carcinoma patients compared with the titers of 139 serum specimens from sex- and age-matched healthy controls. In contrast, both the IgG and IgM serum antibody titers against BPV were significantly decreased for CIN and cervical carcinoma patients compared with those of healthy controls (P less than 0.001 and P less than 0.005, respectively). These results suggest that the difference between IgA and IgG or IgM antibodies to papillomavirus group-specific antigens may represent interesting serological parameters that could possibly be used in the epidemiologic study of women at risk for CIN.
Antibodies, Viral↗
Correction: RuGli cell line not of human origin.
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Animals↗
Detection of IgA antibodies against human papillomavirus in cervical secretions from patients with cervical intraepithelial neoplasia.
Although human papillomavirus (HPV) is involved in the etiology of cervical carcinoma, there are no cervical carcinoma-specific HPV serologic tests available. We investigated the presence of broadly cross-reactive IgA antibodies to papillomavirus (PV) in cervico-vaginal secretions from patients with condylomata and cervical intraepithelial neoplasia (CIN). Purified bovine PV (BPV) virions were used as antigen in an enzyme-linked immunosorbent assay (ELISA). Forty-two women whose ages ranged from 20 to 50 participated in the study. Eight of 9 patients with CIN had IgA antibodies against PV in their cervical secretions. Three of 9 patients with koilocytosis and condylomas but no CIN had IgA antibodies to PV. Six of 24 women with normal Pap-smear and colposcopy also had IgA antibodies against PV in their cervical secretions. The proportion of IgA-positive cervical secretions was significantly higher in the CIN group than in the normal group (p less than 0.005). Our data suggest that IgA antibodies to PV may be a useful marker for CIN.
Adult↗
A synthetic peptide defines a serologic IgA response to a human papillomavirus-encoded nuclear antigen expressed in virus-carrying cervical neoplasia.
The growing awareness of the role of human papillomavirus (HPV) in cervical carcinoma has triggered a search for uncomplicated detection methods. To define a serologic response to HPV, we synthesized peptides based on sequences deduced from the genome of HPV type 16, the most common malignancy-associated type of HPV. One of these peptides reacted with IgA antibodies present in sera from 24 of 33 patients with cervical intraepithelial neoplasia or cervical carcinoma, whereas this peptide reacted with only 6 of 27 sera from individuals without cervical intraepithelial neoplasia. Immunoaffinity-purified human antipeptide IgA antibodies detected HPV-specific 58- and 48-kDa proteins in cervical carcinoma cell extracts and also detected a nuclear antigen in HPV-carrying cervical cancer cell lines and cervical intraepithelial neoplasia biopsied tissue. These antigens were also detected with mouse monoclonal and rabbit polyclonal antibodies to the same peptide. The results indicate that screening for infection with malignancy-associated types of HPV may be possible by simple synthetic peptide-based serology.
Antibodies, Neoplasm↗
The human laminin receptor is a member of the integrin family of cell adhesion receptors.
A receptor for the adhesive basement membrane protein, laminin, was isolated from human glioblastoma cells by affinity chromatography on laminin. This receptor has a heterodimeric structure similar to that of receptors for other extracellular matrix proteins such as fibronectin and vitronectin. Incorporation of the laminin receptor into liposomal membranes makes it possible for liposomes to attach to surfaces coated with laminin. The receptor liposomes also attached to some extent to surfaces coated with fibronectin, but not with other matrix proteins. These properties identify the laminin receptor as a member of the integrin family of cell adhesion receptors.
Antigens, Surface↗
The neurite-promoting domain of human laminin promotes attachment and induces characteristic morphology in non-neuronal cells.
The interaction of cells with laminin and laminin fragments was studied in short-term cell attachment assays. Neurite-promoting chymotrypsin fragments of laminin were isolated using a monoclonal antibody which blocks neurite outgrowth on laminin. The fragments were shown, by electron microscopy after rotary shadowing and by immunological reactivity with different monoclonal antibodies, to contain only the distal end of the long arm. These fragments promoted the attachment and spreading of glioma, sarcoma, carcinoma, muscle, and endodermal cells to the same extent as intact laminin. The attachment was unaffected by peptides containing the RGD sequence. The morphology of the cells on the chymotrypsin fragments was indistinguishable from that on intact laminin but different from the morphology of the same cells on fibronectin. Light microscopy and scanning electron microscopy showed extensive process formation on laminin but not on fibronectin suggestive of increased cell motility in response to laminin. We conclude that the neurite-promoting domain of laminin contains a major site of interaction for non-neuronal cells and that this site induces a cellular response in certain non-neuronal cells that is unique to laminin.
Animals↗