Molecular cloning and sequence analysis of the gene encoding the major merozoite surface antigen of Plasmodium chabaudi chabaudi IP-PC1

Deleersnijder, Willy; Hendrix, Diana; Bendahman, Najib; Hanegreefs, Josée; Brijs, Lea; Hamers-Casterman, C; Hamers, R.

doi:10.1016/0166-6851(90)90148-f

Cited by 31 publications

(7 citation statements)

References 32 publications

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“…Comparison of PbMSP-1 with MSP-1 from human parasites reveals similar information as previously discussed [14,18,19,30] and therefore we will not elaborate. Alignment of MSP-1 from rodent parasites reveals regions of high levels of amino acid identity interrupted by four variable blocks previously designated as VAR I-IV [18]. These variable blocks exhibit little sequence homology between the species, but do exhibit similar amino acid compositions.…”

Section: Discussionmentioning

confidence: 51%

“…1). The boundaries of these variable blocks are similar to the previously identified variable blocks, designated VAR I-IV [18], which correspond to PfMSP-1 variable blocks 4, 8, 10, and 14, respectively (Fig. 2).…”

Section: Cloning and Sequencing Of Msp-1 Genementioning

confidence: 66%

“…MSP-1 from P. 6i6ax [14,15] and from P. chabaudi [16,17] also exhibits intra-species variability. The PcMSP-1 variability consists of four variable blocks, designated as VAR I-IV, which were initially identified as interspecies variable blocks between P. yoelii and P. chabaudi [18]. Comparison of the MSP-1 sequences from P. falciparum, P. 6i6ax and rodent parasites revealed inter-species conserved blocks interspersed with variable blocks [14,19].…”

Section: Introductionmentioning

confidence: 99%

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The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

Jennings

Toebe

Belkum

et al. 1998

Molecular and Biochemical Parasitology

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The complete gene for merozoite surface protein-1 (MSP-1) from Plasmodium berghei has been cloned and sequenced. Comparison of the P. berghei MSP-1 sequence with MSP-1 from other rodent parasites reveals five conserved domains interrupted by four variable blocks. These variable blocks exhibit no sequence homology but do have similar amino acid compositions. Primary proteolytic processing sites are located near the boundaries between the conserved domains and the variable blocks. Sequencing of the variable blocks from several P. berghei isolates shows that the predominant intra-species difference is in the number of tandem repeats. The inter-and intra-species differences suggest that the variable blocks are localized areas with relatively high levels of slipped-strand mispairing, unequal crossing-over, or other intragenic recombination activity. MSP-1 from P. berghei exhibits more repetitiveness than MSP-1 from other species suggesting that P. berghei experiences a higher intrinsic level of events producing variable numbers of tandem repeats or a lower level of events leading to the degeneration of tandem repeats.

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Section: Discussionmentioning

confidence: 51%

Section: Cloning and Sequencing Of Msp-1 Genementioning

confidence: 66%

Section: Introductionmentioning

confidence: 99%

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The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

Jennings

Toebe

Belkum

et al. 1998

Molecular and Biochemical Parasitology

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“…34,35 The Pm and Po MSP1s also harbor imperfect tandem peptide repeats, ranging in size from 2 to 19 amino acids, which are present in two regions of low interspecies similarity flanked between ICBs 7, 9, and 11. An additional repeat domain is observed further downstream for the Po MSP1 in a third non-conserved region between ICBs 11 and 13 ( Figure 1 ).…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of the MSP1 Genes from Plasmodium malariae and Plasmodium ovale

Birkenmeyer¹,

Muerhoff²,

Dawson³

et al. 2010

The American Society of Tropical Medicine and Hygiene

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The merozoite surface protein 1 (MSP1) is the principal surface antigen of the blood stage form of the Plasmodium parasite. Antibodies recognizing MSP1 are frequently detected following Plasmodium infection, making this protein a significant component of malaria vaccines and diagnostic tests. Although the MSP1 gene sequence has been reported for Plasmodium falciparum and Plasmodium vivax, this gene has not been identified for the other two major human-infectious species, Plasmodium malariae and Plasmodium ovale. MSP1 genes from these two species were isolated from Cameroon blood donor samples. The genes are similar in size to known MSP1 genes and encode proteins with interspecies conserved domains homologous to those identified in other Plasmodium species. Sequence and phylogenetic analysis of all available Plasmodium MSP1 amino acid sequences clearly shows that the Po and Pm MSP1 sequences are truly unique within the Plasmodium genus and not simply Pf or Pv variants.

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“…Comparison of the MSP-1 sequence from P. berghei with other rodent parasite MSP-1 sequences [10][11][12] revealed four major interspecies variable regions, or blocks (Jennings et al, in preparation). The first (i.e., most N-terminal) of these variable blocks was cloned from a ugt11 cDNA expression library screened with two different mAbs against PbMSP-1 [13].…”

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confidence: 99%

An additional primary proteolytic processing site in merozoite surface protein-1 of Plasmodium berghei

Wiser

Toebe

Jennings

1997

Molecular and Biochemical Parasitology

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Molecular cloning and sequence analysis of the gene encoding the major merozoite surface antigen of Plasmodium chabaudi chabaudi IP-PC1

Cited by 31 publications

References 32 publications

The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

The complete sequence of Plasmodium berghei merozoite surface protein-1 and its inter- and intra-species variability

Isolation and Characterization of the MSP1 Genes from Plasmodium malariae and Plasmodium ovale

An additional primary proteolytic processing site in merozoite surface protein-1 of Plasmodium berghei

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