Surface antigenic change during differentiation of a parasitic protozoan, Leishmania mexicana: Identification by monoclonal antibodies.

Fong, Dunne; Chang, Kwang-Poo

doi:10.1073/pnas.79.23.7366

Cited by 54 publications

(30 citation statements)

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“…(Etges et al 1986), which is distributed over the entire surface of the promastigote forms, including the flagellum (Fong andChang 1982, Yao et al 2003). Each Leishmania major promastigote in the stationary phase is estimated to have 500,000 copies of gp63, constituting about 1% of the organism's total protein content (Bouvier et al 1985).…”

Section: Gp63 From Leishmaniamentioning

confidence: 99%

The ubiquitous gp63-like metalloprotease from lower trypanosomatids: in the search for a function

Santos

Branquinha

d’Avila-Levy

2006

An. Acad. Bras. Ciênc.

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Plant and insect trypanosomatids constitute the " lower trypanosomatids", which have been used routinely as laboratory models for biochemical and molecular studies because they are easily cultured under axenic conditions, and they contain homologues of virulence factors from the classic human trypanosomatid pathogens. Among the molecular factors that contribute to Leishmania spp. virulence and pathogenesis, the major surface protease, alternatively called MSP, PSP, leishmanolysin, EC 3.4.24.36 and gp63, is the most abundant surface protein of leishmania promastigotes. A myriad of functions have been described for the gp63 from Leishmania spp. when the metacyclic promastigote is inside the mammalian host. However, less is known about the functions performed by this molecule in the invertebrate vector. Intriguingly, gp63 is predominantly expressed in the insect stage of Leishmania, and in all insect and plant trypanosomatids examined so far. The gp63 homologues found in lower trypanosomatids seem to play essential roles in the nutrition as well as in the interaction with the insect epithelial cells. Since excellent reviews were produced in the last decade regarding the roles played by proteases in the vertebrate hosts, we focused in the recent developments in our understanding of the biochemistry and cell biology of gp63-like proteins in lower trypanosomatids.

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Section: Gp63 From Leishmaniamentioning

confidence: 99%

The ubiquitous gp63-like metalloprotease from lower trypanosomatids: in the search for a function

Santos

Branquinha

d’Avila-Levy

2006

An. Acad. Bras. Ciênc.

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“…Experiments using surface biotinylation, cytofluorimetry and immunoelectron microscopy showed that three-quarters of L. mexicana gp63 occur on the cell surface, whereas the re-mainder is located intracellularly [158]. Moreover, gp63 is also released by promastigotes to the extracellular medium in both membrane-associated and free forms [155,159]. Although the GPI anchor can be cleaved in vitro with phospholipase C (PLC) revealing the cross-reacting determinant (CRD) epitope, evidence using antibody against CRD indicates the GPI anchor is not enzymatically cleaved in vivo during the release from the Leishmania cell [160,161].…”

Section: Metallopeptidasesmentioning

confidence: 99%

“…[154], which is distributed over the entire surface of the promastigote forms, including the flagellum [155][156][157]. Each L. major promastigote in the stationary phase is estimated to have 500,000 copies of gp63, constituting about 1% of the organism's total protein content [158].…”

Section: Metallopeptidasesmentioning

confidence: 99%

Biological Roles of Peptidases in Trypanosomatids~!2009-11-26~!2010-02-15~!2010-03-18~!

Vermelho

Branquinha²,

d’Avila-Levy³

et al. 2010

TOPARAJ

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Abstract:In this review, we report the recent developments in the characterization of peptidases and their possible biological functions in the Trypanosomatidae family. The focus will be on peptidases from Trypanosoma cruzi, Leishmania spp., African trypanosomes and plant and insect trypanosomatids. There are numerous events in parasite development where the involvement of peptidases has been established, and they will be approached in the present review. Also in this review we will discuss the central roles have been proposed for peptidases in diverse processes such as virulence, host cell interaction and invasion, catabolism of host proteins, differentiation, cell cycle progression and both stimulation and evasion of host immune responses.

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“…Leishmania spp. harbor a zinc metalloprotease, discovered in the mid-1980s, on their surfaces (14,15,36,37,88). This enzyme, accounting for about 1% of the total protein in promastigotes of Leishmania major and Leishmania mexicana (2, 10) and being potentially important during different stages of the life cycle, soon became the object of much investigation (8,70,71,107).…”

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confidence: 99%

Major Surface Protease of Trypanosomatids: One Size Fits All?

Yao

2010

Infect Immun

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Trypanosomatids are a very diverse group of protozoa including many species of medical, veterinary, and/or economical importance. Leishmania spp. cause disease on the continents of Asia, Africa, Europe, and North and South America; Trypanosoma cruzi is the etiology of Chagas' disease in South and Central America; and Trypanosoma brucei infections result in African sleeping sickness. Four genera of heteroxenous trypanosomatids transmitted by insect vectors infect a wide range of hosts including humans, animals, and plants. Six genera of monoxenous trypanosomatids parasitize numerous species of insects. Due to this diversity, the life cycle of Leishmania spp. is presented as a model to which other heteroxenous and monoxenous groups will be briefly contrasted.During their life cycle, Leishmania spp. shuttle between a flagellated promastigote stage in the sand fly vector and a nonmotile amastigote stage in a mammalian host. During blood meals on infected hosts, the sand fly vectors ingest amastigote-laden macrophages (Mø). These amastigotes transform to procyclic promastigotes in the sand fly gut, multiply by binary fission, and eventually develop into metacyclic promastigotes, the infective stage for mammalian hosts including humans. The sand fly vectors, upon taking another blood meal, inoculate the metacyclic promastigotes into the dermis, where they are phagocytized by Mø of the mammalian hosts. Amastigotes, transformed from metacyclic promastigotes, multiply in parasitophorous vacuoles (PV) of the host's Mø. Multiplication of amastigotes eventually leads to rupture of the infected Mø and release of amastigotes, which infect additional Mø, perpetuating the cycle of replication (38).Other , Crithidia, Leptomonas, Herpetomonas, Rhynchoidomonas, and Phytomonas (87). Leishmania spp. harbor a zinc metalloprotease, discovered in the mid-1980s, on their surfaces (14,15,36,37,88). This enzyme, accounting for about 1% of the total protein in promastigotes of Leishmania major and Leishmania mexicana (2, 10) and being potentially important during different stages of the life cycle, soon became the object of much investigation (8,70,71,107). Although referred to here as major surface protease (MSP), this zinc metalloprotease has also been termed GP63, surface acid protease, promastigote surface protease, EC 3.4.24.36, and leishmanolysin.MSPs of Leishmania spp. belong to the M8 family of endopeptidases, sharing several characteristics with mammalian matrix metalloproteases. Similarities include degradation of the extracellular matrix, cell surface localization, protease activity requiring Zn 2ϩ , and inhibition of protease activity by * Mailing address:

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Surface antigenic change during differentiation of a parasitic protozoan, Leishmania mexicana: Identification by monoclonal antibodies.

Cited by 54 publications

References 18 publications

The ubiquitous gp63-like metalloprotease from lower trypanosomatids: in the search for a function

The ubiquitous gp63-like metalloprotease from lower trypanosomatids: in the search for a function

Biological Roles of Peptidases in Trypanosomatids~!2009-11-26~!2010-02-15~!2010-03-18~!

Major Surface Protease of Trypanosomatids: One Size Fits All?

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