Dr. Laura Klepp
National Institute of Agricultural Technology (INTA), Buenos Aires, Argentina
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Academic Career Length
23Years (2004-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications1 January 2013 in Virulence
Journal Article
MFMarina A. Forrellad
Marina A. Forrellad
Laura KleppAGAndrea Gioffré
Andrea GioffréJGJulia Sabio Y García
Julia Sabio Y García
HMHector R. Morbidoni
Hector R. Morbidoni
FBFabiana Bigi
Fabiana Bigi +2
The Mycobacterium tuberculosis complex (MTBC) consists of closely related species that cause tuberculosis in both humans and animals. This illness, still today, remains to be one of the leading cau...
1 March 2005 in Microbes and Infection
Journal Article
AGAndrea Gioffré
Andrea GioffréEIEduardo Infante
Eduardo Infante
DADiana Aguilar
Diana Aguilar
MSMaría De la Paz Santangelo
María De la Paz Santangelo
Laura KleppFBFabiana Bigi
Fabiana Bigi
+6
1 March 2014 in Tuberculosis
Journal Article
MFMarina Andrea Forrellad
Marina Andrea Forrellad
MMMichael McNeil
Michael McNeil
MSMaría de la Paz Santangelo
María de la Paz Santangelo
FBFederico Carlos Blanco
Federico Carlos Blanco
EGElizabeth García
Elizabeth García
FBFabiana Bigi
Fabiana Bigi +4
Tuberculosis is one of the leading causes of mortality throughout the world. Mycobacterium tuberculosis, the causative agent of human tuberculosis, has developed several strategies involving proteins and other compounds known collectively as virulence factors to subvert human host defences and invade the human host. The Mce proteins are among these virulence-related proteins and are encoded by the mce1, mce2, mce3 and mce4 operons in the genome of M. tuberculosis. It has been proposed that these operons encode ABC-like lipid transporters; however, the nature of their substrates has only been revealed in the case of the Mce4 proteins. Here we found that the knockout of the mce1 operon alters the lipid profile of M. tuberculosis H37Rv and the uptake of palmitic acid. Thin layer chromatography and liquid chromatography-mass spectrometry analysis showed that the mce1 mutant accumulates more mycolic acids than the wild type and complemented strains. Interestingly, this accumulation of mycolic acid is exacerbated when bacteria are cultured in the presence of palmitic acid or arachidonic acid. These results suggest that the mce1 operon may serve as a mycolic acid re-importer.
1 July 2009 in Microbiology
Journal Article
MSMaría de la Paz Santangelo
María de la Paz Santangelo
Laura KleppJNJavier Nuñez-García
Javier Nuñez-García
FBFederico C. Blanco
Federico C. Blanco
MSMarcelo Soria
Marcelo Soria
FBFabiana Bigi
Fabiana Bigi +6
The mce operons constitute four homologous regions in the Mycobacterium tuberculosis genome, each of which has 8–13 ORFs. Although the function of the Mce protein family has not been clearly established, its members are believed to be membrane lipid transporters. Based on functional experiments, we found that the regulator of the mce3 locus, Mce3R, negatively regulates the expression of the Rv1933c–Rv1935c and Rv1936–Rv1941 transcriptional units. These operons are adjacent to one another and divergently transcribed. The predicted functions of most of these genes are related to either lipid metabolism or redox reactions. Bioinformatic analysis of the 5′ UTR sequences of the differentially expressed genes allowed us to define a putative Mce3R motif. Importantly, the Mce3R motif was present six and three times in the mce3R–yrbE3A and Rv1935c–Rv1936 intergenic regions, respectively. Two occurrences of this motif mapped within the two regions of the mce3 operon that were protected by Mce3R in a footprinting analysis, thus indicating that this motif is likely to serve as an operator site for the Mce3R regulator in the promoter. In addition, alterations in the lipid content of M. tuberculosis were detected in the absence of Mce3R. Taken together, these results suggest that Mce3R controls the expression of both the putative transport system encoded in the mce3 operon and the enzymes implicated in the modification of the Mce3-transported substrates.
1 February 2004 in Microbes and Infection
Journal Article
FBFabiana Bigi
Fabiana Bigi
AGAndrea Gioffré
Andrea GioffréLaura KleppMSMaría de la Paz Santangelo
María de la Paz Santangelo
AAAlicia Alito
Alicia Alito
ACAngel Cataldi
Angel Cataldi
+5
1 January 2011 in Tuberculosis
Journal Article
FBFederico Carlos Blanco
Federico Carlos Blanco
MBMaría Verónica Bianco
María Verónica Bianco
VMVirginia Meikle
Virginia Meikle
SGSergio Garbaccio
Sergio Garbaccio
LVLucas Vagnoni
Lucas Vagnoni
FBFabiana Bigi
Fabiana Bigi
+3
About Me
My name is Dr. Laura Inés Klepp and I hold a Ph.D. in Biological Sciences from the University of Buenos Aires (2009), with a specialization in molecular biology and biotechnology. I am currently a Permanent Researcher at INTA (Instituto de Biotecnología, CICVyA) and an Adjunct Researcher at CONICET. Over the past 20 years, I have focused my research on pathogenic Mycobacterium species, particularly on the functional characterization of virulence factors, host-pathogen interactions, and the identification of biomarkers and vaccine candidates to improve tuberculosis control in cattle and related species.
I have authored and co-authored numerous publications in peer-reviewed international journals and presented my work at both national and international scientific conferences. My career includes participation in collaborative projects in Argentina and abroad, including bilateral cooperation programs with India and Slovenia. Alongside my research, I actively contribute to academic training through the supervision of students and teaching of undergraduate and postgraduate courses.
I am a member of the Asociación Argentina de Microbiología and have been awarded fellowships and recognitions from prestigious institutions such as the American Society for Microbiology. My academic interests aim to integrate fundamental microbiology with applied research to generate solutions that strengthen both animal and public health.
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