The major surface glycoprotein (GP63) is present in both life stages of Leishmania

Frommel, Thomas O.; Button, Linda L.; Fujikura, Yoshihisa; McMaster, W. Robert

doi:10.1016/0166-6851(90)90201-v

Cited by 84 publications

(40 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…8, the polyclonal antibody sp180 raised against gp63 recognized, by Western blotting, a major 63-kDa band in total amastigote protein (lane 2) but failed to detect any component present in immunopurified P-8 (lane 4). Moreover, the 63-kDa band detected by sp180 in L. pifanoi amastigotes was localized in the cytoplasmic fraction of the parasite (data not shown), as described by other authors (16,47), rather than the membrane fraction used for P-8 antigen isolation. Another difference is that gp63 has been reported to be resistant to serine proteinase inhibitors (47).…”

Section: Figmentioning

confidence: 62%

Biochemical and Biological Characterization of the ProtectiveLeishmania pifanoiAmastigote Antigen P-8

Colmenares¹,

Tiemeyer

Kima³

et al. 2001

Infect Immun

View full text Add to dashboard Cite

The Leishmania pifanoi amastigote antigen P-8 has been previously shown to induce protective immunity in a murine model of cutaneous leishmaniasis (L. Soong, S. M. Duboise, P. Kima, and D. McMahon-Pratt, Infect. Immun. 63: [3559][3560][3561][3562][3563][3564][3565][3566] 1995). As this antigen is of interest for further vaccine studies, the biochemical characterization of P-8 was undertaken. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Westernblot analysis, and gel filtration chromatography revealed that P-8 antigen consisted of two proteoglycolipid complexes. The P-8 epitope is associated with the L. pifanoi amastigote-specific glycolipid components found in the two complexes. The P-8 complex 1 (P-8c1) consists of a 56-kDa serine metalloproteinase, apolipoprotein E (derived from fetal bovine serum), and amastigote-specific glycolipids. The P-8 complex 2 (P-8c2) consists of a 31-kDa cysteine proteinase associated with amastigote glycolipids. Biochemical analyses suggest that the P-8 antigenic glycolipids may be distinct from previously described Leishmania glycolipids (glycosylinositolphospholipids and sphingoglycolipids). Protective immunity studies revealed that P-8c1 (serine metalloproteinase-glycolipid complex) confers comparable protection against infection as immunopurified P-8. The isolated P-8c2 (cysteine proteinase-glycolipid complex) does not provide significant protection, nor does stimulation with P-8c2 result in significant T-cell activation in P-8-or P-8c2-vaccinated mice. Consequently, the P-8c1 complex appears to be the immunodominant component of P-8.Protozoan parasites of the genus Leishmania are associated with a broad spectrum of diseases, ranging from simple cutaneous to visceral leishmaniasis. Leishmania spp. are dimorphic obligate intracellular parasites. Flagellated promastigotes replicate and differentiate in the gut of the phlebotomine sandfly vector; transmission to humans or other vertebrate hosts occurs when the sandfly takes a blood meal. In the dermis, recently inoculated promastigotes are internalized by phagocytic cells and undergo transformation into amastigotes. Consequently, survival of the parasite within a mammalian host is dependent on successful entry into a macrophage and transformation into the nonmotile amastigote form. Amastigotes maintain the infection within the vertebrate hosts, replicating in the parasitophorous vacuole and eventually leading to the destruction of host cells and invasion of new macrophages.The observations that protective immunity against Leishmania infection can be acquired in susceptible mice (23,25,34,(48)(49)(50) as well as in humans (2, 19, 37) have indicated the possibility for the development of a vaccine against leishmaniasis. In mice, studies of protection against cutaneous leishmaniasis have been observed after immunization with promastigote-derived molecules such as lipophosphoglycan, gp63, defined gp63 epitopes, and gp46 (also known as M-2) (8,20,24,32,45,49,50,58,59). In the search for immunogens that invoke potent host-p...

show abstract

Section: Figmentioning

confidence: 62%

Biochemical and Biological Characterization of the ProtectiveLeishmania pifanoiAmastigote Antigen P-8

Colmenares¹,

Tiemeyer

Kima³

et al. 2001

Infect Immun

View full text Add to dashboard Cite

show abstract

“…The 63 kDa glycoprotein, an important surface protein and common to all species of Leishmania in both forms, amastigote and promastigote [25][26][27], though considered species specific, also reacted against sera of patients with paracoccidioidomycosis.…”

Section: Discussionmentioning

confidence: 99%

Comparison of serological and parasitological methods for cutaneous leishmaniasis diagnosis in the state of Paraná, Brazil

Szargiki¹,

Castro²,

Luz³

et al. 2009

Braz J Infect Dis

View full text Add to dashboard Cite

“…The Leishmania major surface protease (msp or gp63), a zinc endoprotease, is found in all species of Leishmania and is encoded by a family of genes, some of which are tandemly arrayed (Bouvier et al, 1989;Webb et al, 1991). Expression of different copies of the gene is regulated during the development of the parasite and different isoforms of the protein are found in the promastigote stage in the gut of the sand fly and in the amastigote stage in the phagolysosomes of the macrophages (Frommel et al, 1990;Roberts et al, 1995;Ramamoorthy et al, 1995). The major surface protease is thought to play an important role in the virulence of Leishmania by involvement in the degradation of components of the extracellular matrix and by facilitating promastigote attachment to host macrophages (McMaster et al, 1994).…”

Section: Oytnsiysit Vgaldpnwh Pyyseacsan M Y S S G S E Hyivotdina Iddmentioning

confidence: 99%

A Pneumocystis carinii multi-gene family with homology to subtilisin-like serine proteases

1997

View full text Add to dashboard Cite

Medicine, John Radcliffe Hospita't Oxford OX3 9DUtCopies of a multi-gene family, named PRTl (protease 3, encoding a subtilisinlike serine protease were cloned from the opportunistic fungal pathogen Pneumocystis carinii. Comparison of the nucleotide sequence of a genomic clone and a cDNA clone of PRTl from P. carinii f. sp. carinii revealed the presence of seven short introns. Several different domains were predicted from the deduced amino acid sequence: an N-terminal hydrophobic signal sequence, a pro-domain, a subtilisin-like catalytic domain, a P-domain (essential for proteolytic activity), a proline-rich domain, a serinerthreoninerich domain and a C-terminal hydrophobic domain. The catalytic domain showed high homology to other eukaryotic subtilisin-like serine proteases and possessed the three essential residues of the catalytic active site. Karyotypic analysis showed that PRTl was a multi-gene family, copies of which were present on all but one of the P. carinii f. sp. carinii chromosomes. The different copies of the PRTl genes showed nucleotide sequence heterogeneity, the highest level of divergence being in the proline-rich domain, which varied in both length and composition. Some copies of PRTl were contiguous with genes encoding the P. carinii major surface glycoprotein. UK

show abstract

The major surface glycoprotein (GP63) is present in both life stages of Leishmania

Cited by 84 publications

References 21 publications

Biochemical and Biological Characterization of the ProtectiveLeishmania pifanoiAmastigote Antigen P-8

Biochemical and Biological Characterization of the ProtectiveLeishmania pifanoiAmastigote Antigen P-8

Comparison of serological and parasitological methods for cutaneous leishmaniasis diagnosis in the state of Paraná, Brazil

A Pneumocystis carinii multi-gene family with homology to subtilisin-like serine proteases

Contact Info

Product

Resources

About