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Epitope specificity as a prime deter...

Kelly-Quintos, Casie Anne.

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Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG./
Author:	Kelly-Quintos, Casie Anne.
Description:	125 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2356.
Contained By:	Dissertation Abstracts International67-05B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3217784
ISBN:	9780542693014

Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG.
Kelly-Quintos, Casie Anne.

Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG. - 125 p.

Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2356.

Thesis (Ph.D.)--Harvard University, 2006.

Poly N-Acetyl Glucosamine (PNAG) is a surface expressed polysaccharide that is a known virulence factor of Staphylococcus aureus and recently shown to be expressed by numerous pathogenic bacteria. PNAG was previously demonstrated to be the target of protective antibodies when used as a vaccine in animal studies; however, no reports of the human antibody response to PNAG have been published. This dissertation describes the importance of epitope specificity in the human immune response to PNAG. The PNAG molecule is N-acetylated and therefore this dissertation analyzes the contribution of both acetate dependant and acetate independent epitopes to the ability of antibodies specific to these epitopes to opsonize S. aureus. This dissertation demonstrates that antibodies specific to the deacetylated epitopes on PNAG have more opsonic and protective activity against S. aureus by using S. aureus colonized CF patient serum and human monoclonal antibodies (mAbs) specific to different epitopes on PNAG. A possible mechanism explaining the superiority of deacetylated PNAG (dPNAG) specific antibodies is shown with the elucidation of the function of the IcaB protein as a deacetylase that is required for the cell association of PNAG. Overall, this dissertation suggests that vaccination or treatment with dPNAG or dPNAG specific antibodies respectively will be the most effective means of targeting PNAG on staphylococcus or other PNAG expressing bacteria for opsonophagocytosis.

ISBN: 9780542693014Subjects--Topical Terms:

1017734
Biology, Microbiology.

Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG.
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100 1 $a Kelly-Quintos, Casie Anne. $3 1917910
245 1 0 $a Epitope specificity as a prime determinant of the opsonic and protective activity of human antibodies to the bacterial surface polysaccharide PNAG.
300 $a 125 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2356.
500 $a Adviser: Gerald B. Pier.
502 $a Thesis (Ph.D.)--Harvard University, 2006.
520 $a Poly N-Acetyl Glucosamine (PNAG) is a surface expressed polysaccharide that is a known virulence factor of Staphylococcus aureus and recently shown to be expressed by numerous pathogenic bacteria. PNAG was previously demonstrated to be the target of protective antibodies when used as a vaccine in animal studies; however, no reports of the human antibody response to PNAG have been published. This dissertation describes the importance of epitope specificity in the human immune response to PNAG. The PNAG molecule is N-acetylated and therefore this dissertation analyzes the contribution of both acetate dependant and acetate independent epitopes to the ability of antibodies specific to these epitopes to opsonize S. aureus. This dissertation demonstrates that antibodies specific to the deacetylated epitopes on PNAG have more opsonic and protective activity against S. aureus by using S. aureus colonized CF patient serum and human monoclonal antibodies (mAbs) specific to different epitopes on PNAG. A possible mechanism explaining the superiority of deacetylated PNAG (dPNAG) specific antibodies is shown with the elucidation of the function of the IcaB protein as a deacetylase that is required for the cell association of PNAG. Overall, this dissertation suggests that vaccination or treatment with dPNAG or dPNAG specific antibodies respectively will be the most effective means of targeting PNAG on staphylococcus or other PNAG expressing bacteria for opsonophagocytosis.
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