Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Published reports indicate that HIV is recovered from BAL fluid of patients with AIDS who have LIP but not with other AIDS-related pulmonary disease. Our experience has been different. Ten BAL specimens from nine patients with AIDS were cultured directly in peripheral blood mononuclear cells, and all ten cultures were positive for HIV as indicated by examination of the culture supernatant by reverse transcriptase assay and enzyme immunoassay for HIV antigen. Five of the specimens were also positive for Pneumocystis carinii, and other pulmonary diagnoses included histoplasmosis, lymphoma, Kaposi's sarcoma, and aspiration pneumonia. Five additional BAL specimens were cultured after freezing at -70 degrees C, but only two were culture-positive for HIV (p = 0.022; FET). This study indicates that HIV can be recovered from the BAL fluid in most patients with AIDS, unrelated to the type of pulmonary disease. In contrast to cultures, HIV antigen was detected in the BAL fluid of only one patient, and that patient had LIP with noncaseating granulomas. Therefore, HIV culture is not useful in the diagnosis of LIP, but HIV antigen detection should be studied further. All BAL fluids should be considered potentially infectious.
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PMID:Recovery of human immunodeficiency virus and detection of p24 antigen in bronchoalveolar lavage fluid from adult patients with AIDS. 250 Mar 12

Histoplasma capsulatum is the etiological agent of histoplasmosis, a chronic respiratory infection that is generally asymptomatic in healthy individuals, but severe or fatal in patients who are immunosuppressed or otherwise debilitated. H. capsulatum is found as a mould in soil and becomes a pathogenic yeast in the mammalian host. The first line of defense that H. capsulatum faces during host invasion is the attack of polymorphonuclear neutrophils and resident macrophages. In animal models, once phagocytosed, H. capsulatum is not killed by fusion of the phago-lysosomes, instead it multiplies within non-activated macrophages and destroys them. Upon induction of cell-mediated immunity, cytokines activate macrophages and destroy the yeast cells. Some aspects of the fungus-macrophage interaction have been elucidated, and it is clear that some of the mechanisms by which H. capsulatum escapes the lethal effects of this very hostile environment, involve the regulation of specific genes. Recently, using the differential display reverse transcriptase polymerase chain reaction technique, a number of H. capsulatum genes that are induced after the yeasts are ingested by macrophages have been identified. However, the mechanisms that underlie the capacity of H. capsulatum to adapt to the new environmental conditions present in macrophages remain to be clarified.
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PMID:Host response and Histoplasma capsulatum/macrophage molecular interactions. 1120 77

gp43 is the major diagnostic antigen of Paracoccidioides brasiliensis, the agent of paracoccidioidomycosis (PCM) in humans. In the present study, cDNA of the gp43 gene (PbGP43) was obtained by reverse transcriptase PCR, inserted into a pGEX vector in frame with the glutathione S-transferase (GST) gene, and expressed in Escherichia coli as inclusion bodies. Immunoblotting showed that all sera from patients with chronic pulmonary and acute lymphatic forms of PCM reacted with the recombinant fusion protein of the mature gp43 (381 amino acids). Reactivity with fusion proteins containing subfragments of the N-terminal, internal, or C-terminal regions occurred eventually, and the C-terminal region was the most antigenic. Lack of reactivity with the subfragments may be due to the conformational nature of the gp43 epitopes. Sera from patients with aspergillosis, candidiasis, and histoplasmosis did not react with the gp43-GST fusion protein. Our results suggest that recombinant gp43 corresponding to the processed antigen can be a useful tool in the diagnosis of PCM.
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PMID:Expression in bacteria of the gene encoding the gp43 antigen of paracoccidioides brasiliensis: immunological reactivity of the recombinant fusion proteins. 1241 50

Heat shock protein 60 (hsp60) were isolated from several fungal, protozoal and many bacterial pathogens and successfully used for protective vaccination in some infection models. This work focuses on the isolation of recombinant hsp60 from the dermatophyte, Trichophyton mentagrophytes as a potentially protective antigen in trichophytosis. With the help of a previously tested set of degenerated primers, it was used reverse transcriptase polymerase chain reaction (RT-PCR) for isolation of partial cDNA of the hsp60 T. mentagrophytes (labelled hsp60-TM814), which was cloned into cloning vector. The sequencing of hsp60-TM814 cDNA and global alignment confirmed homology of the hsp60-TM814 with other members of the hsp60 family. Hsp60-TM814 cDNA corresponds to the region encoding the immunoprotective fragment of the hsp60 from Histoplasma capsulatum, used successfully in mouse model of histoplasmosis. A recombinant fragment (r-hsp60-TM664), 220 amino acids in length, was prepared in a prokaryote expression system, and its identity confirmed by mass spectroscopy. High immunogenicity of r-hsp60-TM664 was proven after subcutaneous immunization of mice. Immunized mouse sera recognized r-hsp60-TM664 on Western blots as well as hsp60 from mouse liver lysate and lysate of Candida albicans.
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PMID:Isolation and characterization of an immunogenic fragment of heat shock protein 60 from Trichophyton mentagrophytes. 1560 54