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The potential of a probiotic-derived antimicrobial peptide for the control of vaginal pathogens
Descriptive
TypeOfResource
Text
TitleInfo
(ID = T-1)
Title
The potential of a probiotic-derived antimicrobial peptide for the control of vaginal pathogens
Identifier
ETD_3067
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000057702
Language
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(type = code)
eng
Genre
(authority = marcgt)
theses
Subject
(ID = SBJ-1);
(authority = RUETD)
Topic
Food Science
Subject
(ID = SBJ-2);
(authority = ETD-LCSH)
Topic
Vagina--Diseases
Subject
(ID = SBJ-3);
(authority = ETD-LCSH)
Topic
Probiotics
Subject
(ID = SBJ-4);
(authority = ETD-LCSH)
Topic
Bacteriocins
Subject
(ID = SBJ-5);
(authority = ETD-LCSH)
Topic
Bacterial vaginitis
Abstract
(type = abstract)
Bacterial vaginosis (BV) is characterized by replacement of vaginal probiotics with several anaerobic pathogens. This condition can lead to numerous complications during pregnancy and labor. It is also a risk factor for HIV acquisition. Currently-available antibiotic treatments for BV are notorious for having a high (30-40%) rate of reoccurrence; therefore alternative treatments are critically desired. A multiple-hurdle approach involving bacteriocins may provide such an alternative. Previous studies indicate that lactocin 160, a bacteriocin produced by Lactobacillus rhamnosus, a vaginal probiotic, is active against BV - associated Gardnerella vaginalis and Prevotella bivia. The objective of the current study is to understand the mode of action of lactocin 160 against G. vaginalis and to seek out other natural antimicrobials exhibiting
synergistic activity with this bacteriocin. Our results demonstrate that lactocin 160 targets the cytoplasmic membrane of G. vaginalis, causing the efflux of ATP molecules and dissipation of both, ΔΨ and ΔpH components of proton motive force. Based on these
results, we presume that like many other known bacteriocin-like substances, lactocin 160 triggers formation of transient pores in the cytoplasmic membranes of its target cells. The interactions between lactocin 160 and four other natural antimicrobials in the ability to inhibit G. vaginalis were evaluated using the checkerboard assay. Our results indicate that zinc lactate and soapnut extract act synergistically with lactocin 160 against this pathogen and therefore have a potential to be successfully used as the components of the multiple-hurdle antimicrobial formulation for the treatment of BV.
synergistic activity with this bacteriocin. Our results demonstrate that lactocin 160 targets the cytoplasmic membrane of G. vaginalis, causing the efflux of ATP molecules and dissipation of both, ΔΨ and ΔpH components of proton motive force. Based on these
results, we presume that like many other known bacteriocin-like substances, lactocin 160 triggers formation of transient pores in the cytoplasmic membranes of its target cells. The interactions between lactocin 160 and four other natural antimicrobials in the ability to inhibit G. vaginalis were evaluated using the checkerboard assay. Our results indicate that zinc lactate and soapnut extract act synergistically with lactocin 160 against this pathogen and therefore have a potential to be successfully used as the components of the multiple-hurdle antimicrobial formulation for the treatment of BV.
PhysicalDescription
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electronic resource
Extent
xi, 152 p. : ill.
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application/pdf
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text/xml
Note
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Ph.D.
Note
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Includes bibliographical references
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Includes vita
Note
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by Yevgeniy Turovskiy
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Turovskiy
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Yevgeniy
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1977-
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author
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Yevgeniy Turovskiy
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Chikindas
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Michael
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chair
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Advisory Committee
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Michael Chikindas
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(type = personal)
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(type = family)
Takhistov
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(type = given)
Paul
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internal member
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Advisory Committee
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Paul Takhistov
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Lee
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Tung-Ching
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internal member
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Advisory Committee
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Tung-Ching Lee
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Badmaev
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Vladimir
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outside member
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Advisory Committee
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Vladimir Badmaev
Name
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NamePart
Rutgers University
Role
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degree grantor
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Graduate School - New Brunswick
Role
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school
OriginInfo
DateCreated
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2011
DateOther
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(type = degree)
2011-01
Place
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(type = code)
xx
RelatedItem
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
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ETD
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Title
Graduate School - New Brunswick Electronic Theses and Dissertations
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rucore19991600001
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(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T3SF2VTK
Genre
(authority = ExL-Esploro)
ETD doctoral
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Rights
RightsDeclaration
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder
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(type = personal)
Name
FamilyName
Turovskiy
GivenName
Yevgeniy
Role
Copyright Holder
RightsEvent
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Type
Permission or license
DateTime
2010-12-21 12:53:03
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Copyright holder
Name
Yevgeniy Turovskiy
Affiliation
Rutgers University. Graduate School - New Brunswick
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Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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Technical
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ETD
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application/pdf
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application/x-tar
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1914880
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