Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani

Choudhury, Rajdeep; Bhaumik, Siddhartha Kumar; De, Tanmay; Chakraborti, Tapati

doi:10.1007/s11010-008-9849-7

Cited by 18 publications

(10 citation statements)

References 55 publications

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“…Our previous study demonstrated that a 115-kDa serine protease is secreted by an Indian strain of L. donovani (8). In the present report, we have demonstrated the intracellular localization of this parasite-derived secreted serine protease and also its differential expression in virulent, avirulent, and attenuated strains of L. donovani as well as in different cell cycle stages of the parasite.…”

supporting

confidence: 66%

“…The migration of the parasite in host tissues is mediated by the release of proteolytic enzymes that can degrade the tissue barriers. Potent proteolytic enzymes of cysteine, serine, and metalloprotease classes have been identified in secretory products of many of the parasites (8,19,26,27,30). Serine proteases have been reported to have strong hydrolytic activity against a wide range of extracellular matrix (ECM) components and human plasma proteins; hence, they are thought to play vital roles in the host tissue invasion process (17).…”

mentioning

confidence: 99%

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In SituImmunolocalization and Stage-Dependent Expression of a Secretory Serine Protease inLeishmania donovaniand Its Role as a Vaccine Candidate

Choudhury

Das

Bhaumik

et al. 2010

Clin Vaccine Immunol

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Proteases have been found to play essential roles in many biological processes, including the pathogenesis of leishmaniasis. Most parasites rely on their intracellular and extracellular protease repertoire to invade and multiply in mammalian host cells. However, few studies have addressed serine proteases in Leishmania and their role in host pathogenesis. Here we report the intracellular distribution of a novel L. donovani secretory serine protease in the flagellar pocket, as determined by immunogold labeling. Flow cytometry and confocal immunofluorescence analysis revealed that the expression of the protease diminishes sequentially from virulent to attenuated strains of this species and is also highly associated with the metacyclic stage of L. donovani promastigotes. The level of internalization of parasites treated with the anti-115-kDa antibody into host macrophages was significantly reduced from that of non-antibody-treated parasites, suggesting that this serine protease probably plays a role in the infection process. In vivo studies confirmed that this serine protease is a potential vaccine candidate. Altogether, the 115-kDa serine protease might play vital roles in L. donovani pathogenesis and hence could be recognized as a potential candidate for drug design.Leishmania species, belonging to the family Trypanosomatidae, are a group of protozoan pathogens that cause a spectrum of chronic diseases ranging from self-healing cutaneous lesions to a lethal visceral disorder. They represent a major health problem in tropical and subtropical areas around the world. Leishmania species have a relatively simple life cycle, with parasite stage differentiation regulated by environmental signals encountered in their different hosts. They are digenetic parasites: the flagellated promastigote forms, which can be derived in axenic culture, differentiate within the alimentary tracts of sandfly vectors from a replicating procyclic to a nonreplicating, infectious metacyclic stage, whereas obligately intracellular amastigotes live and replicate in mammalian mononuclear phagocytes, such as macrophages (1).Recent advances in genomic analysis of several of the major global parasites have revealed key factors involved in the pathogenesis of parasite diseases. Among the major virulence factors identified are parasite-derived proteases. Parasite proteases play significant roles in the pathogenesis of parasitic diseases; the proteases are involved in the invasion of the host via parasite migration through tissue barriers, degradation of host proteins for their nutrition, immune evasion, and activation of inflammation (21). The migration of the parasite in host tissues is mediated by the release of proteolytic enzymes that can degrade the tissue barriers. Potent proteolytic enzymes of cysteine, serine, and metalloprotease classes have been identified in secretory products of many of the parasites (8,19,26,27,30). Serine proteases have been reported to have strong hydrolytic activity against a wide range of extracellular matrix (ECM) c...

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confidence: 66%

mentioning

confidence: 99%

In SituImmunolocalization and Stage-Dependent Expression of a Secretory Serine Protease inLeishmania donovaniand Its Role as a Vaccine Candidate

Choudhury

Das

Bhaumik

et al. 2010

Clin Vaccine Immunol

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“…A similar serine protease was found in the supernatant culture of L. donovani with the same molecular weight of 115 KDa [27] and with the same localization, mainly in flagelar pockets by immunohistochemistry [28]. The expression of the protease was correlated to a high virulence for the parasite and to the metacyclic stage of L. donovani promastigotes [28].…”

Section: Secreted Serine Protease (Psp) From L Donovanimentioning

confidence: 60%

Serine Proteases and Vaccines against Leishmaniasis: A Dual Role

Chaves¹,

Gomes²,

De-Simone³

et al. 2012

J Vaccines Vaccin

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Serine proteases are involved in several biochemical processes that are essential for the biology of pathogens, including Leishmania sp. Considering their importance, an interest in serine proteases for vaccine development against leishmaniasis has been raised. As targets, these enzymes have demonstrated a dual role in a vaccine against leishmaniasis, both protective and a counter-protective, depending on the conditions that they are evaluated. In this work, serine proteases or inhibitors of them that have been used as components of vaccines to Leishmania sp. are presented, aiming to disseminate the knowledge gained about these proteases and their potential in potential vaccine against leishmaniasis.

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“…A released enzyme of 110 kDa was also identified and seems to occur as a homodimer [187]. Similar enzymes were also identified in L. braziliensis [188] and L. donovani [189]. A common feature of these enzymes seems to be their ability to digest a wide range of proteinaceous substrates and several enzymes are homodimeric or heterodimeric proteins.…”

Section: Serine Peptidasesmentioning

confidence: 61%

Biological Roles of Peptidases in Trypanosomatids

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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Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani

Cited by 18 publications

References 55 publications

In SituImmunolocalization and Stage-Dependent Expression of a Secretory Serine Protease inLeishmania donovaniand Its Role as a Vaccine Candidate

In SituImmunolocalization and Stage-Dependent Expression of a Secretory Serine Protease inLeishmania donovaniand Its Role as a Vaccine Candidate

Serine Proteases and Vaccines against Leishmaniasis: A Dual Role

Biological Roles of Peptidases in Trypanosomatids

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