Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using nonradioactive hybridization, the multilocal probes 33.15, F10 and (CAC)5 were shown to recognize multiple minisatellite regions in nuclear DNA of Leishmania, producing on Southern blots complex banding patterns typical of DNA fingerprints. We used the 33.15 probe to study 14 different strains belonging to 6 different species from both the sub-genus Viannia and the Leishmania mexicana complex of the sub-genus Leishmania. Distinct DNA fingerprints were obtained for each strain, permitting their identification. On the other hand, each strain showed little or no clonal variation. The information from the fingerprinting maps could be used for constructing phenograms and cladograms of the species and strains of Leishmania.
Mol Biochem Parasitol 1992 Jul
PMID:DNA fingerprints: a tool for identification and determination of the relationships between species and strains of Leishmania. 150 45

Immunization with the GP46/M-2 membrane glycoprotein of Leishmania amazonensis has been shown to induce a protective immune response against infection. We have surveyed a variety of trypanosomatid species and genera for the presence and expression of this gene family, information that will be relevant to future vaccine studies against leishmaniasis. Molecular karyotype analysis revealed the presence of GP46/M-2 genes in all members of the Leishmania mexicana complex, Leishmania major, Leishmania donovani, Leishmania tarentolae, and Crithidia fasciculata. In contrast, DNAs from species of the Leishmania braziliensis complex (L. braziliensis, Leishmania guyanensis, and Leishmania panamensis) failed to hybridize to GP46/M-2 probes. Western blot analyses with several polyclonal antisera against the GP46/M-2 protein revealed protein expression in L. major and L. donovani, but not L. panamensis or L. braziliensis. Phylogenetic analysis suggests that a loss of the GP46A gene family occurred following separation of the L. braziliensis complex, prior to speciation events within this complex. These data indicate that GP46/M-2 membrane glycoprotein may not be critical to parasite survival, but may play an ancillary role during the developmental cycle.
Mol Biochem Parasitol 1992 Jan
PMID:Loss of the GP46/M-2 surface membrane glycoprotein gene family in the Leishmania braziliensis complex. 154 9

A developmentally regulated cysteine proteinase associated with an unique lysosomal organelle, the megasome, has been described for the intracellular amastigotes of the Leishmania mexicana complex; this proteinase appears to be important in the survival of the parasite. Degenerate primers encoding the active sites residues have been used to amplify cysteine proteinase cDNA sequences from axenically cultured amastigotes of Leishmania pifanoi, a member of the L. mexicana complex. Based on sequence data, two distinct genes (Lpcys1 and Lpcys2) were identified. Although both genes are preferentially transcribed in the amastigote stage, each is distinct in genomic arrangement and chromosome location, with Lpcys2 showing evidence for the presence of 8-20 tandemly arrayed copies and mRNA levels 10-fold higher than Lpcys1. Related forms of the Lpcys1 and Lpcys2 genes exist in other species of the genus Leishmania, including Leishmania braziliensis, Leishmania major and Leishmania donovani. The protein sequence of an abundant immunoaffinity purified amastigote cysteine proteinase (A-2) is identical to that predicted for the product of Lpcys2; immunofluorescence studies show an intracellular pattern/distribution for the A-2 proteinase consistent with a putative megasomal association. The DNA sequence of a genomic copy of Lpcys2 predicts a C-terminal extension for the proteinase; comparative sequence analyses of the C-terminal extensions found for Trypanosoma cruzi and Trypanosoma brucei reveal the selective conservation of cysteine, as well as proline and glycine residues, suggesting that conservation of folding and secondary structure may be required for biological function.
Mol Biochem Parasitol 1993 Jan
PMID:Identification of two distinct cysteine proteinase genes of Leishmania pifanoi axenic amastigotes using the polymerase chain reaction. 842 6