Antigens with Repeated Amino Acid Sequences from the Asexual Blood Stages of Plasmodium falciparum

1988 ◽  
pp. 148-172
Author(s):  
R.F. Anders ◽  
R.L. Coppel ◽  
G.V. Brown ◽  
D.J. Kemp
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Amino Acid Sequences

Structural and antigenic polymorphism of the 35- to 48-kilodalton merozoite surface antigen (MSA-2) of the malaria parasite Plasmodium falciparum

1991 ◽  
Vol 11 (2) ◽  
pp. 963-971
Author(s):  
B Fenton ◽  
J T Clark ◽  
C M Khan ◽  
J V Robinson ◽  
D Walliker ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Surface Antigen ◽  
Dna Sequences ◽  
Amino Acid Sequences ◽  
Merozoite Surface Antigen ◽  
Parasite Plasmodium ◽  
Genes Encoding ◽  
Parasite Plasmodium Falciparum ◽  
Group B

Merozoite surface antigen MSA-2 of the human parasite Plasmodium falciparum is being considered for the development of a malaria vaccine. The antigen is polymorphic, and specific monoclonal antibodies differentiate five serological variants of MSA-2 among 25 parasite isolates. The variants are grouped into two major serogroups, A and B. Genes encoding two different variants from serogroup A have been sequenced, and their DNA together with deduced amino acid sequences were compared with sequences encoded by other alleles. The comparison shows that the serological classification reflects differences in DNA sequences and deduced primary structure of MSA-2 variants and serogroups. Thus, the overall homologies of DNA and amino acid sequences are over 95% among variants in the same serogroup. In contrast, similarities between the group A variants and a group B variant are only 70 and 64% for DNA and amino acid sequences, respectively. We propose that the MSA-2 protein is encoded by two highly divergent groups of alleles, with limited additional polymorphism displayed within each group.

Amino acid sequences recognized by T cells: studies on a merozoite surface antigen from the FCQ-27/PNG isolate of Plasmodium falciparum

1990 ◽  
Vol 25 (1-3) ◽  
pp. 155-163 ◽  
Author(s):  
C.M. Rzepczyk ◽  
P.A. Csurhes ◽  
E.P. Baxter ◽  
T.J. Doran ◽  
D.O. Irving ◽  
...  
Keyword(s):  
T Cells ◽  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Surface Antigen ◽  
Amino Acid Sequences ◽  
Merozoite Surface Antigen

scholarly journals Structural and antigenic polymorphism of the 35- to 48-kilodalton merozoite surface antigen (MSA-2) of the malaria parasite Plasmodium falciparum.

1991 ◽  
Vol 11 (2) ◽  
pp. 963-971 ◽  
Author(s):  
B Fenton ◽  
J T Clark ◽  
C M Khan ◽  
J V Robinson ◽  
D Walliker ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Surface Antigen ◽  
Dna Sequences ◽  
Amino Acid Sequences ◽  
Merozoite Surface Antigen ◽  
Parasite Plasmodium ◽  
Genes Encoding ◽  
Parasite Plasmodium Falciparum ◽  
Group B

Merozoite surface antigen MSA-2 of the human parasite Plasmodium falciparum is being considered for the development of a malaria vaccine. The antigen is polymorphic, and specific monoclonal antibodies differentiate five serological variants of MSA-2 among 25 parasite isolates. The variants are grouped into two major serogroups, A and B. Genes encoding two different variants from serogroup A have been sequenced, and their DNA together with deduced amino acid sequences were compared with sequences encoded by other alleles. The comparison shows that the serological classification reflects differences in DNA sequences and deduced primary structure of MSA-2 variants and serogroups. Thus, the overall homologies of DNA and amino acid sequences are over 95% among variants in the same serogroup. In contrast, similarities between the group A variants and a group B variant are only 70 and 64% for DNA and amino acid sequences, respectively. We propose that the MSA-2 protein is encoded by two highly divergent groups of alleles, with limited additional polymorphism displayed within each group.

scholarly journals THE CIDR1α-PfEMP1 SEQUENCE FROM INDONESIAN PLASMODIUM FALCIPARUM AND ITS POTENTIAL ASSOCIATION WITH THE CEREBRAL OUTCOME

2021 ◽  
Vol 7 (1) ◽  
pp. 34-39
Author(s):  
Erma Sulistyaningsih ◽  
Yunita Armiyanti ◽  
Rosita Dewi
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Cerebral Malaria ◽  
Severe Malaria ◽  
Sequence Similarity ◽  
Malaria Diagnosis ◽  
Severe Case ◽  
Amino Acid Sequences ◽  
Pcr Product ◽  
Potential Association

Background: Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) is an important protein responsible for the pathogenesis of severe malaria, including cerebral malaria. The protein is highly diverse. The CIDR1α-PfEMP1 binds endothelial protein receptor (EPCR) and may associated with the brain swelling in childhood malaria. Objective: To analyze the CIDR1α-PfEMP1 from Indonesian isolate and determine its association with cerebral malaria outcome. Methods: Fifteen blood samples of clinically mild to severe malaria-patient were collected for DNA extraction. Malaria diagnosis was conducted microscopically by Giemsa-stained thin blood smear. The CIDR1α domain was amplified by PCR using specific primer and PCR product was sequenced. The nucleotide sequences were analyzed by NCBI blast, DNASIS MAX 3 and translated into amino acid sequences using Expasy Translation Tool. Results: One out of fifteen samples was severe malaria case and infected with P. falciparum, the rest were clinically mild to moderate malaria and infected with pure P. falciparum or mixed infection of P. falciparum and P. vivax. Amplification for CIDR1α domain resulted a single band of + 550 bp from a severe sample only. Sequencing of PCR product on both strands read 524 nucleotides and BLAST analysis confirmed as CIDR1α sequence. Multiple alignment showed 74-78% nucleotide sequence similarity with reference sequences, but amino acid sequences presented 23.5% homologous. Conclusion: An identified CIDR1α domain only from severe case implicating the potential association with the severe outcome including cerebral malaria, but the highly diverse of the domain needs further studies on the interaction with the pathological-causing receptor in the host.

Immune sera recognize on erythrocytes a Plasmodium falciparum antigen composed of repeated amino acid sequences

Nature ◽  
1984 ◽  
Vol 310 (5980) ◽  
pp. 789-792 ◽  
Author(s):  
Ross L. Coppel ◽  
Alan F. Cowman ◽  
Robin F. Anders ◽  
Albert E. Bianco ◽  
Robert B. Saint ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Amino Acid Sequences

scholarly journals Antibodies to repeated amino acid sequences in Pf155, a merozoite associated antigen of plasmodium falciparum

1986 ◽  
Vol 81 (suppl 2) ◽  
pp. 77-81 ◽  
Author(s):  
Klavs Berzins ◽  
Hedvig Perlmann ◽  
Birgitta Wahlin ◽  
Wipaporn Ruangjirachuporn ◽  
Birthe Högh ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Amino Acid Sequences

Diversity of Primary Structures of the Carboxy-terminal Regions of Mammalian Fibrinogen Aα-Chains

1993 ◽  
Vol 69 (04) ◽  
pp. 351-360 ◽  
Author(s):  
Masahiro Murakawa ◽  
Takashi Okamura ◽  
Takumi Kamura ◽  
Tsunefumi Shibuya ◽  
Mine Harada ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rhesus Monkey ◽  
Syrian Hamster ◽  
Tandem Repeats ◽  
Mammalian Species ◽  
Amino Acid Sequences ◽  
Point Of View ◽  
Cross Linking ◽  
Amino Terminal ◽  
Rgd Sequence

SummaryThe partial amino acid sequences of fibrinogen Aα-chains from five mammalian species have been inferred by means of the polymerase chain reaction (PCR). From the genomic DNA of the rhesus monkey, pig, dog, mouse and Syrian hamster, the DNA fragments coding for α-C domains in the Aα-chains were amplified and sequenced. In all species examined, four cysteine residues were always conserved at the homologous positions. The carboxy- and amino-terminal portions of the α-C domains showed a considerable homology among the species. However, the sizes of the middle portions, which corresponded to the internal repeat structures, showed an apparent variability because of several insertions and/or deletions. In the rhesus monkey, pig, mouse and Syrian hamster, 13 amino acid tandem repeats fundamentally similar to those in humans and the rat were identified. In the dog, however, tandem repeats were found to consist of 18 amino acids, suggesting an independent multiplication of the canine repeats. The sites of the α-chain cross-linking acceptor and α2-plasmin inhibitor cross-linking donor were not always evolutionally conserved. The arginyl-glycyl-aspartic acid (RGD) sequence was not found in the amplified region of either the rhesus monkey or the pig. In the canine α-C domain, two RGD sequences were identified at the homologous positions to both rat and human RGD S. In the Syrian hamster, a single RGD sequence was found at the same position to that of the rat. Triplication of the RGD sequences was seen in the murine fibrinogen α-C domain around the homologous site to the rat RGDS sequence. These findings are of some interest from the point of view of structure-function and evolutionary relationships in the mammalian fibrinogen Aα-chains.

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