Literature DB >> 11551627

The 235 kDa rhoptry protein of Plasmodium (yoelii) yoelii: function at the junction.

S M Khan1, W Jarra, P R Preiser.   

Abstract

All malaria parasites are obligate intracellular organisms that must clearly recognise and discriminate between different cells during their life cycle. Invasion into a cell is a multi-step event that is marked by initial attachment proceeding to irreversible junction formation and penetration. A 235 kDa rhoptry protein (Py235) in the rodent malaria, Plasmodium yoelii yoelii has been shown to be involved in red blood cell (rbc) binding and is involved in a new mechanism of clonal phenotypic variation that may be important in adaptation and immune evasion. Immunisation studies using Py235 have also revealed a role for this protein in the virulence phenotype seen with P. y. yoelii in laboratory mice. Interestingly, the genes that encode this protein are present as a multi-gene family. In this paper, we examine Py235 at the level of DNA, transcription and expression, discussing the role of this protein during invasion, in virulence and in immune evasion.

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Year:  2001        PMID: 11551627     DOI: 10.1016/s0166-6851(01)00333-4

Source DB:  PubMed          Journal:  Mol Biochem Parasitol        ISSN: 0166-6851            Impact factor:   1.759


  12 in total

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Journal:  EMBO J       Date:  2003-03-03       Impact factor: 11.598

5.  Passive immunization with a multicomponent vaccine against conserved domains of apical membrane antigen 1 and 235-kilodalton rhoptry proteins protects mice against Plasmodium yoelii blood-stage challenge infection.

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6.  Changes in parasite virulence induced by the disruption of a single member of the 235 kDa rhoptry protein multigene family of Plasmodium yoelii.

Authors:  Devaki Bapat; Ximei Huang; Karthigayan Gunalan; Peter R Preiser
Journal:  PLoS One       Date:  2011-05-20       Impact factor: 3.240

7.  A comprehensive evaluation of rodent malaria parasite genomes and gene expression.

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10.  PfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptor.

Authors:  Marilis Rodriguez; Sara Lustigman; Estrella Montero; Yelena Oksov; Cheryl A Lobo
Journal:  PLoS One       Date:  2008-10-01       Impact factor: 3.240

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