RESUMO
Antinuclear autoantibodies (ANA) are highly informative biomarkers in autoimmune diagnostics. The increasing demand for effective test systems, however, has led to the development of a confusingly large variety of different platforms. One of them, the indirect immunofluorescence (IIF), is regarded as the common gold standard for ANA screening, as described in a position statement by the American College of Rheumatology in 2009. Technological solutions have been developed aimed at standardization and automation of IIF to overcome methodological limitations and subjective bias in IIF interpretation. In this review, we present the EUROPattern Suite, a system for computer-aided immunofluorescence microscopy (CAIFM) including automated acquisition of digital images and evaluation of IIF results. The system was originally designed for ANA diagnostics on human epithelial cells, but its applications have been extended with the latest system update version 1.5 to the analysis of antineutrophil cytoplasmic antibodies (ANCA) and anti-dsDNA antibodies.
Assuntos
Anticorpos Antinucleares/análise , Sistemas Computacionais , Técnica Indireta de Fluorescência para Anticorpo/métodos , Interpretação de Imagem Assistida por Computador/instrumentação , Microscopia de Fluorescência/métodos , Automação , Biomarcadores , Humanos , Armazenamento e Recuperação da Informação , Padrões de Referência , Reprodutibilidade dos Testes , SoftwareRESUMO
Candida albicans is the primary etiologic agent of candidiasis, a disease that can vary from superficial mucosal lesions to life-threatening systemic or disseminated diseases. Strains of C. albicans have been reported to possess long, thin filamentous protein cell surface appendages termed fimbriae (R.B. Gardiner, M. Canton, and A. W. Day, Bot. Gaz. 143:534-541, 1982). These fimbriae were isolated, purified, and partially characterized. The major structural subunit of the fimbriae is a glycoprotein which consists of 80 to 85% carbohydrate (consisting primarily of D-mannose) and 10 to 15% protein. The molecular weight of the glycosylated fimbrial subunit is approximately 66,000, while unglycosylated protein has an approximate molecular weight of 8,644. The fimbriae function as adhesins mediating C. albicans binding to human buccal epithelial cells. Amino acid analysis of the purified fimbrial subunit indicates that the fimbrial subunit is composed of 50% hydrophobic amino acid residues. The N terminus of the fimbrial subunit is blocked to N-terminal sequencing.