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001 ocn148084167;

003 OCoLC;

005 20251021154320.0;

008 070629s2004 xx a bm 000 0 eng d;

035 a| (Sirsi) o148084167;

035 a| (OCoLC)148084167;

049 a| EREE;

050 4 a| QL568.V5b| M67 2004;

100 1 a| Morris, Phillip Ray,e| author.?| UNAUTHORIZED;

245 10 a| Cloning and characterization of the cDNA encoding the antigen 5 allergen from two species of paper wasp (Polistes dominulus and Polistes exclamans) /c| by Phillip Ray Morris.;

264 0 c| 2004.;

300 a| 76 leaves :b| illustrations ;c| 28 cm;

336 a| textb| txt2| rdacontent;

337 a| unmediatedb| n2| rdamedia;

338 a| volumeb| nc2| rdacarrier;

502 b| M.S.c| East Carolina Universityd| 2004;

500 a| Presented to the faculty of the Department of Biology.;

500 a| Advisor: Donald R. Hoffman;

500 a| Advisor: Margit Schmidt;

520 3 a| Hymenoptera venoms are complex mixtures of proteins, peptides and other organic molecules, many with pharrriacological properties. Many of these compounds can cause toxic and allergic reactions in humans. Wasps, hornets and yellow jackets comprise a group of insects known as vespids. Four vespid venom proteins are known allergens. They are hyaluronidase, phospholipase A1B, protease and antigen 5. Homologous proteins from different vespid species have similar properties including molecular weights and amino acid compositions. Vespid allergic individuals often have sensitivities to several different species and this multiple-sensitivity can be a consequence of immunologic cross reactivity to these homologous proteins. In this study, the nucleotide sequence of the venom allergen antigen 5 (Ag5) of two species of paper wasp {Polistes dominulus and Polistes exclamans) was obtained using molecular biological techniques. These sequences were compared to nucleotide sequences of other vespids Ag 5s to determine the percent similarity. The percent similarities were then compared to the degree of cross-reactivity demonstrated by wasp antigen 5 with hornet and yellow jacket antigen 5 molecules. The nucleotide sequences were translated to amino acid sequences and protein analysis was performed. A computer generated model of the structure of the Ag5 protein was created from the peptide sequences. The obtained cDNA sequences will be expressed to produce a recombinant protein to be used in further studies.;

504 a| Includes bibliographical references (leaves 71-76).;

650 0 a| Paper waspsx| Genetics.=| ^A827614;

650 0 a| DNA-binding proteins.=| ^A260138;

650 0 a| Insect allergy.=| ^A717622;

650 2 a| DNA-Binding Proteins.0| (DNLM)D004268=| ^A926280;

655 2 a| Academic Dissertation.0| (DNLM)D019478?| UNAUTHORIZED;

650 7 a| DNA-binding proteins.2| fast0| (OCoLC)fst00886613;

650 7 a| Insect allergy.2| fast0| (OCoLC)fst00973974;

655 7 a| Academic theses.2| fast0| (OCoLC)fst01726453;

655 7 a| Academic theses.2| lcgft;

655 7 a| Thèses et écrits académiques.2| rvmgf0| (CaQQLa)RVMGF-000001173;

700 1 a| Hoffman, Donald R.,e| degree supervisor.=| ^A1024891;

700 1 a| Schmidt, Margit,e| degree supervisor.=| ^A1469024;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/12611;

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949 a| Click on web addressw| asish| hsl111;

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596 a| 1 4;

998 a| 1086312;

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Cloning and characterization of the cDNA encoding the antigen 5 allergen from two species of paper wasp (Polistes dominulus and Polistes exclamans) / by Phillip Ray Morris.

Author/creator	Morris, Phillip Ray author.
Other author	Hoffman, Donald R., degree supervisor.
Other author	Schmidt, Margit, degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	2004.
Description	76 leaves : illustrations ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Paper wasps--Genetics. DNA-binding proteins. Insect allergy. DNA-Binding Proteins.

Summary	Hymenoptera venoms are complex mixtures of proteins, peptides and other organic molecules, many with pharrriacological properties. Many of these compounds can cause toxic and allergic reactions in humans. Wasps, hornets and yellow jackets comprise a group of insects known as vespids. Four vespid venom proteins are known allergens. They are hyaluronidase, phospholipase A1B, protease and antigen 5. Homologous proteins from different vespid species have similar properties including molecular weights and amino acid compositions. Vespid allergic individuals often have sensitivities to several different species and this multiple-sensitivity can be a consequence of immunologic cross reactivity to these homologous proteins. In this study, the nucleotide sequence of the venom allergen antigen 5 (Ag5) of two species of paper wasp {Polistes dominulus and Polistes exclamans) was obtained using molecular biological techniques. These sequences were compared to nucleotide sequences of other vespids Ag 5s to determine the percent similarity. The percent similarities were then compared to the degree of cross-reactivity demonstrated by wasp antigen 5 with hornet and yellow jacket antigen 5 molecules. The nucleotide sequences were translated to amino acid sequences and protein analysis was performed. A computer generated model of the structure of the Ag5 protein was created from the peptide sequences. The obtained cDNA sequences will be expressed to produce a recombinant protein to be used in further studies.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: Donald R. Hoffman
General note	Advisor: Margit Schmidt
Dissertation note	M.S. East Carolina University 2004
Bibliography note	Includes bibliographical references (leaves 71-76).
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

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Cloning and characterization of the cDNA encoding the antigen 5 allergen from two species of paper wasp (Polistes dominulus and Polistes exclamans) / by Phillip Ray Morris.

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