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A 5-year retrospective multicenter study was performed for microascaceous moulds (Microascaceae, Ascomycetes) in Finnish clinical specimens. The files from 1993-1997 of six clinical mycology laboratories in Finland were searched for reports of these fungi, mainly Scopulariopsis and Scedosporium anamorphs in keratinous specimens. From the 521 primary findings, 165 cases were selected for further study based on direct microscopy, colony numbers and accompanying fungi. The clinical records of 148 cases (141 Scopulariopsis, 7 Scedosporium) were studied. Of the nail infections from which Scopulariopsis was recovered, 39 cases were further separated which showed clinical or laboratory-based evidence of dermatophytosis. In the remaining 90 'non-dermatophyte' nail cases, Scopulariopsis spp. were the only documented fungal agents (c. 6 cases/million/year). The patients were mainly elderly, 66% of whom had problems involving their big toe nails. For 74% of them, the nail problem was mentioned as their reason for visiting the physician. However, only 18% had documented benefit from treatment. The Scopulariopsis nail infections seem to be treatment-resistant and the pathogenesis and etiological role of Scopulariopsis remain poorly understood.

The aetiology of lichen planus is unknown, but it is often connected with infections. In recent years peptic ulcer disease has also been closely linked with an infectious agent, Helicobacter pylori. A case-control study was conducted in 78 patients with lichen planus to find out a previous history of peptic ulcer disease, using a questionnaire and a medical record review. Patients were also asked about family history in first- and second-degree relatives. Fifty-seven patients with other skin diseases were interviewed as controls. The prevalence of H. pylori infection in patients with lichen planus was compared to that of 39 patients with other skin diseases and to the overall prevalence rates of H. pylori infection in Finland. Our findings are consistent with an approximately three-fold increased risk of peptic ulcer in patients with chronic/repeating lichen planus, when compared to the control patients (p = 0.04) and also to the overall peptic ulcer prevalence rates in Finland. Forty-one percent of the patients with chronic/repeating lichen planus had a first- or second-degree family member with a peptic ulcer, while the corresponding rate in the control group was only 12% (p=0.003). The prevalence of H. pylori infection in patients with chronic/repeating lichen planus and transient lichen planus was not significantly different from that in patients with other skin diseases.

The antibody response of patients with gluten-sensitive enteropathy and dermatitis herpetiformis against alcohol-soluble prolamines of wheat, rye, barley, oats and corn assessed by immunoblotting was compared to the staining patterns produced by monoclonal antigliadin antibodies. Both monoclonal antibodies (MAbs) and patient serum reacted with wheat, rye, barley and oats, the patient serum showing individual variation both in IgA and IgG stainings. A broad reactivity with polypeptides from 30 to 68 kD was, however, typical for patient serum and comparable to the reactivity of two broadly reacting antigliadin MAbs. This kind of broad reactivity of the MAb may suggest that it binds to glutamine-repeating sequences of highly homologous gliadin polypeptides. Glutamine- and proline-containing motifs Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro are also included in the peptides toxic to the celiac small intestinal mucosa. Our study indicates that the humoral response of the patients may detect similar structures, in oat prolamines as well. Patient serum and one of the MAbs also reacted with a 22-kD polypeptide of corn extract. The meaning of this reactivity is not known, and further characterization of the antigenic epitopes of different cereals will be important.

X3, a monoclonal antibody of unusual specificity, is described. This antibody reacts with one or more cytokeratin polypeptides and also reacts with an avian (chicken, quail) nuclear antigen that appears to be present in all cell types (chicken) tested, although with variable staining pattern and intensity. This antigen is distinct from the cytokeratins but does have an epitope in common with this class of proteins. It disappears from the nucleus during the early stages of cell division and reappears during anaphase as a granular cytoplasmic structure. In late telophase the antigen is relocated in the nucleus. This antigen, which we have designated as avian-specific nuclear antigen ( AVNA ), is not associated with chromatin or ribonucleoproteins. From immunoblotting experiments on chicken fibroblast nuclei, AVNA is probably a complex composed of one or several polypeptides, one of which has a molecular weight of approximately 60 kD. The proteins were identified as nuclear matrix proteins rather than pore complex-lamina proteins by immunoblotting experiments on the purified nuclear matrix of chicken erythrocytes. The major polypeptide had a molecular weight of 60 kD and the minor polypeptide a molecular weight of 69 kD.

SUMMARY An immunofluorescence method using whole sections of wheat grains as the substrate was applied to detect circulating antibodies to wheat gluten in dermatitis herpetiformis patients and in controls. Only IgG class antibodies were detected. From dermatitis herpetiformis patients 22% had these antibodies as had 22% of the atopic dermatitis group. Among the controls who had no skin problems 12% were faintly positive. It is evident that the test as such is non-specific and does not have diagnostic significance in dermatitis herpetiformis.

The serum samples of 27 children with dermatitis herpetiformis (DH) were examined for the presence of antigliadin (AGA) and antireticulin (ARA) antibodies. AGA were determined with an enzyme-linked immunosorbent assay (ELISA) and ARA with an immunofluorescence method. Increased IgA or IgG class AGA levels were found in four of ten children on a normal diet, in two of 25 on a gluten-free diet (GFD), and in two of four children on gluten challenge. The corresponding figures for ARA were nine of ten, two of 25, and four of four, respectively. All nine patients with ARA on a normal diet had either subtotal or partial villous atrophy, whereas the patient negative for ARA had a normal jejunal mucosa. ARA were mostly of IgA class, and after gluten withdrawal, increased levels fell to normal range. Four children were challenged with gluten, and they all developed subtotal villous atrophy and demonstrated IgA class ARA. These results suggest that in childhood DH, ARA is a more sensitive indicator of gluten-sensitive enteropathy than AGA, but both antibody determinations can be used in monitoring adherence to GFD treatment.

A sensitive and technically simple enzyme-linked immunosorbent assay (ELISA) was developed to demonstrate circulating IgA- and IgG-class antibodies to gliadin, a component of wheat gluten. Serum samples from 24 patients with dermatitis herpetiformis (DH), 5 with coeliac disease (CD) and 75 normal controls were analysed. Antigliadin antibodies (AGA) of the IgA class were detected in 71% of DH patients, all of the CD patients and 19% of the controls. IgG-AGA was found in over 90% of DH patients and controls and in all of the CD patients. The mean ELISA values of both IgA- and IgG-class AGA were significantly higher in DH patients than in the controls. The occurrence of circulating IgA-class AGA is compatible with the hypothesis that these antibodies can be deposited in the skin, e.g. as immune complexes, or due to cross-reactivity of gliadin and dermal reticulin.

SUMMARY Circulating IgA-class anti-endomysium antibodies (EmA) can be detected by indirect immunofiuorescence on monkey oesophagus sections. We found EmA in 22 (76%) of 29 patients with dermatitis herpetiformis (DH) on a normal, gluten-containing diet. The highest frequency (100%) of EmA was observed in patients with sub-total villous atrophy. IgA-class antigliadin antibodies (AGA) were found using an ELISA method in 59% of 29 DH patients and in 86% of those with sub-total villous atrophy. There was a significant correlation between EmA litres and AGA levels in individual patients. Gluten-free diet (GFD) treatment caused a rapid decrease in EmA litres; only three of the 12 patients still showed raised EmA after 6–12 months on a GFD and two of these three had failed to adhere to a strict diet. In contrast, no decrease in EmA titres occurred in four patients maintained on a normal diet, and two of the three patients with initially negative EmA developed positive titres when continuing on a normal diet. These results show that both IgA-class EmA and AGA are good indicators of jejunal damage in DH. The rapid fall of EmA titres after gluten withdrawal indicates that this test is also useful for monitoring a patient's adherence to a GFD.

A monoclonal antibody is described which reacts with the intermediate filament proteins vimentin, desmin, keratins, actin, and myosin. This is the first report of an epitope common to intermediate filament proteins and myosin. X1, the wide-spectrum monoclonal antibody in question, was isolated in the course of screening monoclonal antibodies to chicken thymocytes. Cross-reactivities were investigated by immunofluorescence on various types of cultured cells and sectioned tissues, ELISA with a panel of purified antigens, immunoprecipitation, immunodot tests, and immunoblotting.

Antigliadin antibodies (AGA) were analyzed by immunoblotting from the sera of 30 patients with dermatitis herpetiformis (DH) and of 13 patients with gluten-sensitive enteropathy (GSE). The results were correlated to the jejunal morphology and to the serum AGA values as quantified with an enzyme-linked immunosorbent assay (ELISA). Immunoblotting analysis disclosed a distinct pattern of AGA which was similar in patients with DH and GSE. In both diseases individual variation in IgG class AGA patterns was large, suggesting that several antigenic determinants are involved in the AGA response. The IgA class AGA pattern was clearly more homogeneous. The sera with several bands in immunoblotting had the highest AGA levels in ELISA. Strong staining in the main gliadin area (bands from 31 to 38 kd) indicated severely damaged intestinal mucosa whereas the serum of DH patients with partial villous atrophy or normal mucosa showed usually weaker staining. The immunoblotting pattern of sera from healthy controls was even weaker but was directed against the same polypeptides as in the patients suggesting a quantitative rather than qualitative difference between healthy and diseased subjects. This difference was, however, more obvious in the IgA than in the IgG class AGA pattern possibly indicating a more fundamental defect in the regulation of synthesis of IgA isotype in DH and GSE.

Antigliadin antibodies in serum samples of 31 children with coeliac disease were measured by an enzyme-linked immunosorbent technique. In young patients (less than 2 years) tested before gluten withdrawal IgA antigliadin antibody levels were invariably above the levels of 36 controls. The titres fell rapidly when gluten was eliminated from the diet and rose on its reintroduction. The titres were not always greater than the control level in older untreated patients. IgA antigliadin antibodies seem to be a good marker of the immune reaction in the jejunum triggered by gluten. In 2 IgA-deficient patients gluten challenge caused an increase in IgM antigliadin antibodies, and at the same time the number of IgM-containing cells increased in the jejunal mucosa. Rising IgG antigliadin antibody levels after gluten elimination were seen in 6 patients, 5 of whom had very low complement C3 levels before gluten elimination.