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Y Hillman

Publications and source records attributed to Y Hillman.

8 recordsLinked to original sources
PubMed1988

An S antigen gene from Plasmodium falciparum contains a novel repetitive sequence.

The complete sequence of the gene coding for the S antigen from the Wellcome (West African) strain of Plasmodium falciparum has been obtained. It contains a central repetitive region consisting of 65 copies of a partially degenerate 24 bp sequence, coding for a conserved 8 amino acid repeat (Gly Pro Asn Ser Asp Gly Asp Lys). The repeat sequence is different from those of S antigens characterised in other strains and thus represents a new S antigen serotype.

Amino Acid Sequence↗
PubMed1987

Processing of the precursor to the major merozoite surface antigens of Plasmodium falciparum.

Specific sequences derived from the gene for the precursor to the major merozoite surface antigens (PMMSA) of Plasmodium falciparum have been expressed in Escherichia coli and the products have been used to produce antibodies. These antibodies, together with monoclonal antibodies, have been used to investigate the form of the PMMSA protein associated with merozoites. Polypeptide fragments derived by processing from the PMMSA protein have been detected in extracts of merozoites and assigned to locations within the PMMSA coding sequence.

Animals↗
PubMed1986

Structural diversity of the major surface antigen of Plasmodium falciparum merozoites.

The structures of the major merozoite surface antigen of Plasmodium falciparum and the gene encoding it were indistinguishable for the Wellcome strain and the Thai clone T9/94 but different for clones T9/96, T9/98, and T9/101. The central portion of the gene is subject to the greatest variation in structure. The protein from all five lines was found to be posttranslationally modified by covalent addition of both carbohydrate and fatty acid.

Animals↗
PubMed1984

Expression of cloned cDNA for a major surface antigen of Plasmodium falciparum merozoites.

A cDNA library of P. falciparum was constructed. Using size-selected mRNA as a probe several clones were isolated which hybridized to mRNAs larger than 5 kilobases (kb). The cDNA insert of pFC 17, which hybridizes to 5.6-kb mRNA was expressed by fusion to anthranilate synthetase I in a plasmid expression vector. The expressed fusion protein was shown to contain epitopes of a 195-kDa protein which is the precursor to 3 major surface antigens of P. falciparum merozoites.

Animals↗
PubMed1984

Cloning of malarial genes coding for high molecular weight antigens: isolation of fragments of Plasmodium falciparum genes coding for proteins of 145 000 molecular weight.

RNA preparations from Plasmodium falciparum were shown to direct the cell free synthesis of many high molecular weight proteins, some of which could be immunoprecipitated by sera from humans immune to P. falciparum. Among these was an abundant protein with a molecular weight of 145 000. Messenger RNAs coding for high molecular weight antigens were enriched by size fractionation and used after reverse transcription to identify genomic restriction fragments in Southern blots. Genomic restriction fragments were cloned into plasmid and phage lambda vectors. Two recombinants which were recognized by the high molecular weight probe were characterized by hybrid-select-translation. In both cases the predominant in vitro translation products were proteins with a molecular weight of 145 000.

Animals↗
PubMedDate not supplied

Primary structure of the precursor to the three major surface antigens of Plasmodium falciparum merozoites.

Recently, a class of protein antigens of high relative molecular mass (Mt) which can induce protective immunity against blood-stage malaria has been identified. In Plasmodium falciparum the protein has a Mr of approximately 195,000 (P195). It is the precursor of three proteins of Mr 83,000 (83K), 42K and 19K which are the major surface antigens of merozoites; thus it may also be useful for immunization against P. falciparum. Three studies describing the isolation of single short complementary DNA clones for part of the P195 gene sequence have been reported. Here we describe the complete structure of the P195 gene determined from further DNA clones, its organization within genomic DNA and the location of the specific processing fragments within the primary amino-acid sequence.

Amino Acid Sequence↗