Karina Tuz

Illinois Institute of Technology

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Oscar Juárez

Illinois Institute of Technology

Pingdong Liang

Illinois Institute of Technology

Xuan Fang

Peking University

Daniel A. Raba

Michigan State University

Ming Yuan

Sixth Affiliated Hospital of Sun Yat-sen University

Russell J. Ferland

University of New England

David D. L. Minh

Illinois Institute of Technology

Yuyao Hu

Illinois Institute of Technology

Herminia Pasantes‐Morales

Universidad Nacional Autónoma de México

Rodrigo Franco

University of Nebraska–Lincoln

Cooperative Institutions

Weatherford College

180

Centre Hospitalier de Beauvais

173

Sumitomo Electric Industries (United States)

168

Illinois Institute of Technology

Universidad Nacional Autónoma de México

University of Washington

National Institutes of Health

Albany Medical Center Hospital

Seattle University

Rensselaer Polytechnic Institute

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Mutations in CSPP1 Cause Primary Cilia Abnormalities and Joubert Syndrome with or without Jeune Asphyxiating Thoracic Dystrophy

The American Journal of Human Genetics (2013)

Karina Tuz Ruxandra Bachmann‐Gagescu Diana R. O’Day Kiet Hua Christine R. Isabella

Ciliopathy

Joubert syndrome

Ciliogenesis

Ciliopathies

Haploinsufficiency

Nephronophthisis

Morpholino

Intraflagellar Transport

10.1016/j.ajhg.2013.11.019

Cite

Citations (108)

Supplementary data for the manuscript titled 'Energy metabolism and aerobic respiratory chain of Vitreoscilla sp. C1: Comparison with beta-proteobacteria'

Zenodo (CERN European Organization for Nuclear Research) (2023)

Paul T. Nguyen Yuyao Hu Anne Caroline Mascarehas Dos Santos Alexander M. Shuppara Pingdong Liang

This dataset contains the supplementary data files for the manuscript titled, 'Energy metabolism and aerobic respiratory chain of Vitreoscilla sp. C1: Comparison with beta-proteobacteria.'

BETA (programming language)

10.5281/zenodo.7754389

Cite

Citations (0)

Role of Subunit D in Ubiquinone-Binding Site of Vibrio cholerae NQR: Pocket Flexibility and Inhibitor Resistance

ACS Omega (2019)

Daniel A. Raba Ming Yuan Xuan Fang William M. Menzer Bing Xie

The ion-pumping NADH: ubiquinone dehydrogenase (NQR) is a vital component of the respiratory chain of numerous species of marine and pathogenic bacteria, including Vibrio cholerae. This respiratory enzyme couples the transfer of electrons from NADH to ubiquinone (UQ) to the pumping of ions across the plasma membrane, producing a gradient that sustains multiple homeostatic processes. The binding site of UQ within the enzyme is an important functional and structural motif that could be used to design drugs against pathogenic bacteria. Our group recently located the UQ site in the interface between subunits B and D and identified the residues within subunit B that are important for UQ binding. In this study, we carried out alanine scanning mutagenesis of amino acid residues located in subunit D of V. cholerae NQR to understand their role in UQ binding and enzymatic catalysis. Moreover, molecular docking calculations were performed to characterize the structure of the site at the atomic level. The results show that mutations in these positions, in particular, in residues P185, L190, and F193, decrease the turnover rate and increase the Km for UQ. These mutants also showed an increase in the resistance against the inhibitor HQNO. The data indicate that residues in subunit D fulfill important structural roles, restricting and orienting UQ in a catalytically favorable position. In addition, mutations of these residues open the site and allow the simultaneous binding of substrate and inhibitors, producing partial inhibition, which appears to be a strategy used by Pseudomonas aeruginosa to avoid autopoisoning.

Alanine scanning

Paracoccus denitrificans

Alanine

10.1021/acsomega.9b02707

Cite

Citations (7)

Mechanisms of Cell Volume Regulation in Hypo-osmolality

The American Journal of Medicine (2006)

Herminia Pasantes‐Morales Ruth Lezama Gerardo Ramos‐Mandujano Karina Tuz

Osmolyte

Osmotic concentration

10.1016/j.amjmed.2006.05.002

Cite

Citations (144)

The Joubert Syndrome-associated Missense Mutation (V443D) in the Abelson-helper Integration Site 1 (AHI1) Protein Alters Its Localization and Protein-Protein Interactions

Journal of Biological Chemistry (2013)

Karina Tuz Yi-Chun Hsiao Oscar Juárez Bingxing Shi Erin Y. Harmon

Missense mutations in AHI1 result in the neurodevelopmental ciliopathy called Joubert syndrome.Mutations in AHI1 decrease cilia formation, alter its localization and stability, and change its binding to HAP1 and NPHP1.Mutations in AHI1 affect ciliogenesis, AHI1 protein localization, and AHI1-protein interactions.This study begins to describe how missense mutations in AHI1 can cause Joubert syndrome. Mutations in AHI1 cause Joubert syndrome (JBTS), a neurodevelopmental ciliopathy, characterized by midbrain-hindbrain malformations and motor/cognitive deficits. Here, we show that primary cilia (PC) formation is decreased in fibroblasts from individuals with JBTS and AHI1 mutations. Most missense mutations in AHI1, causing JBTS, occur in known protein domains, however, a common V443D mutation in AHI1 is found in a region with no known protein motifs. We show that cells transfected with AHI1-V443D, or a new JBTS-causing mutation, AHI1-R351L, have aberrant localization of AHI1 at the basal bodies of PC and at cell-cell junctions, likely through decreased binding of mutant AHI1 to NPHP1 (another JBTS-causing protein). The AHI1-V443D mutation causes decreased AHI1 stability because there is a 50% reduction in AHI1-V443D protein levels compared with wild type AHI1. Huntingtin-associated protein-1 (Hap1) is a regulatory protein that binds Ahi1, and Hap1 knock-out mice have been reported to have JBTS-like phenotypes, suggesting a role for Hap1 in ciliogenesis. Fibroblasts and neurons with Hap1 deficiency form PC with normal growth factor-induced ciliary signaling, indicating that the Hap1 JBTS phenotype is likely not through effects at PC. These results also suggest that the binding of Ahi1 and Hap1 may not be critical for ciliary function. However, we show that HAP1 has decreased binding to AHI1-V443D indicating that this altered binding could be responsible for the JBTS-like phenotype through an unknown pathway. Thus, these JBTS-associated missense mutations alter their subcellular distribution and protein interactions, compromising functions of AHI1 in cell polarity and cilium-mediated signaling, thereby contributing to JBTS.

Joubert syndrome

Ciliogenesis

Ciliopathy

Intraflagellar Transport

Mutant protein

10.1074/jbc.m112.420786

Cite

Citations (33)

NRJ Media as the Gold-Standard Arcobacter-Specific Detection System: Applications in Poultry Testing

Frontiers in Microbiology (2022)

Paul T. Nguyen Karina Tuz Lawrence Restaino Oscar Juárez

Arcobacter species are ubiquitous emerging pathogens with an impact that has been underestimated due to limitations in isolation and detection methods. Our group recently developed the novel NRJ Arcobacter -detection system, with major improvements in specificity and selectivity compared to other culture-based methods. In this work, the NRJ detection system was evaluated using retail whole broiler chicken carcass. Nanopore 16S rRNA gene amplicon sequencing demonstrated that Arcobacter species are found in very low abundance in retail chicken and that indigenous microbiota could be a major factor interfering with detection. Comparison of the microbiome obtained from modified Houf broth (HB) method, as the standard detection system, and the novel NRJ method, showed Arcobacter abundances of <15% and >97%, respectively. The NRJ system significantly inhibits the growth of non-target microbiota, and specifically allows the multiplication of Arcobacter species. In this report, we describe the gold-standard of Arcobacter -specific culture-based method to test food matrices, which can be used for other applications, such as clinical and environmental sampling.

Arcobacter

Gold standard (test)

Poultry meat

10.3389/fmicb.2022.903079

Cite

Citations (2)

Comparison of Two Culture-Based Detection Systems for the Isolation of Arcobacter butzleri, Arcobacter cryaerophilus, and Arcobacter skirrowii in Raw Ground Poultry

Journal of Food Protection (2023)

Paul T. Nguyen Karina Tuz Oscar Juárez Lawrence Restaino

Arcobacters are emerging pathogens that have been underestimated due to a lack of a standardized isolation method. The aim of this research was to evaluate the ability to isolate Arcobacter butzleri, Arcobacter cryaerophilus, and Arcobacter skirrowii using two Arcobacter-specific culture detection systems: (i) the Houf broth and modified charcoal cefoperazone deoxycholate agar supplemented with cefoperazone, amphotericin B, and teicoplanin (HB/mCCDA+CAT), and (ii) the Nguyen-Restaino-Juárez Arcobacter enrichment broth and chromogenic agar (NRJ-B/M). Both detection systems were evaluated for productivity ratio, sensitivity, and specificity. As a result, the productivity ratio for both plating agars were >90%, which indicates that the selective agents used in the two plating agars did not inhibit Arcobacter growth. Moreover, sensitivity evaluations using artificially inoculated retail ground poultry (n = 780) determined that both detection systems were able to isolate A. butlzeri with >95% sensitivity at the 0.1 and 1.0-2.0 CFU/g detection level. The sensitivity in A. cryaerophilus isolation was higher for NRJ-B/M (78.0% at 0.1 CFU/g; 95.1% at 1.0-2.0 CFU/g) when compared with HB/mCCDA+CAT (34.1% at 0.1 CFU/g; 51.2% at 1.0-2.0 CFU/g). Both detection systems resulted in <50% sensitivity when isolating A. skirrowii at 0.1 and 1.0-2.0 CFU/g; however, the sensitivity for NRJ-B/M was significantly higher than HB/mCCDA+CAT. At the detection level of 5.0 CFU/g, both detection systems were able to isolate A. skirrowii with 100% sensitivity. Specificity comparisons using uninoculated ground poultry samples (n = 40) indicated the growth of background microbiota were significantly inhibited or could be easily differentiated on NRJ-B/M (90.0%, specificity) when compared with HB/mCCDA+CAT (30.0%, specificity). Overall, these results show that the NRJ-B/M detection system is a more sensitive and specific detection system when isolating Arcobacter spp. from ground chicken.

Arcobacter

Cefoperazone

Isolation

10.1016/j.jfp.2023.100057

Cite

Citations (0)

Hyposmolarity evokes norepinephrine efflux from synaptosomes by a depolarization‐ and Ca²⁺‐dependent exocytotic mechanism

European Journal of Neuroscience (2005)

Karina Tuz H. Pasantes‐Morales

Abstract Osmolarity reduction (20%) elicited 3 H‐norepinephrine (NE) efflux from rat cortical synaptosomes. The hyposmotic NE release resulted from the following events: (i) a Na + ‐dependent and La 3+ ‐, Gd 3+ ‐ and ruthenium red‐sensitive depolarization; (ii) a cytosolic Ca 2+ ([Ca 2+ ] i ) rise with contributions from external Ca 2+ influx and internal Ca 2+ release, probably through the mitochondrial Na + –Ca 2+ exchanger; and (iii) activation of a [Ca 2+ ] i ‐evoked, tetanus toxin (TeTX)‐sensitive, PKC‐modulated NE efflux mechanism. This sequence was established from results showing a drop in the hyposmotic [Ca 2+ ] i rise by preventing depolarization with La 3+ , and by the inhibitory effects of Ca 2+ ‐free medium (EGTA; 50%), CGP37157 (the mitochondrial Na + –Ca 2+ exchanger blocker; 48%), EGTA + CGP37157 or by EGTA‐AM (> 95% in both cases). In close correspondence with these effects, NE efflux was 92% decreased by Na + omission, 75% by La 3+ , 47% by EGTA, 50% by CGP37157, 90% by EGTA + CGP37157 and 88% by EGTA‐AM. PKC influenced the intracellular Ca 2+ release and, mainly through this action, modulated NE efflux. TeTX suppressed NE efflux. The K + ‐stimulated NE release, studied in parallel, was unaffected by Na + omission, or by La 3+ , Gd 3+ or ruthenium red. It was fully dependent on external Ca 2+ , insensitive to CGP37157 and abolished by TeTX. These results suggest that the hyposmotic events, although different from the K + ‐evoked depolarization and [Ca 2+ ] i rise mechanisms, are able to trigger a depolarization‐dependent, Ca 2+ ‐dependent and TeTX‐sensitive mechanism for neurotransmitter release.

EGTA

Ruthenium red

Efflux

Channel blocker

10.1111/j.1460-9568.2005.04344.x

Cite

Citations (14)

Signaling events during swelling and regulatory volume decrease.

Neurochemical Research (2000)

Herminia Pasantes‐Morales Velia Cardin Karina Tuz

Osmolyte

Second messenger system