Personal Information
Ashish Solanki

Department of Medicine, Medical University of South Carolina, Charleston, South Caroina, USA

Ashish Solanki
Educations
From 2009 to 2014, Doctorate , India
From 2006 to 2008, M.Sc. (Biotechnology) , India
From 2002 to 2005, B.Sc. (Botany, Hons.) , India
Work Experiences
From 2015 to 2016, Postdoc , Medical University of South Carloina, Charleston, SC, USA
Projects
From 2013 to 2014, Accurate, accelerated and affordable kit to predict the pre-term and post-partum recovery” , We have developed a diagnosis kit to measure the level of a vital protein in human plasma. Also, I have experience of working on developing different affinity coating protocols including IgG, DNA aptamer based (screening and validation) and small molecule (peptide) based methods as well.
From 2009 to 2013, Structure analysis of proteins and their complexes involved in host-pathogen interaction in HIV infection , Global shape analysis of HIV-1 neutralizing antibody IgG1 b12 confirmed that this neutralizing antibody is inherently rigid and is asymmetric in solution. • In pursuit of engineering mAbs for neutralization, employed structural and biochemical studies including SAXS, AUC, SEC-MALS, limited proteolysis, ELISA, Western blot analysis etc to elucidate the differences in the shapes of 17 HIV-1 neutralizing and nonneutralizing mAbs. Complexes of mAbs with gp120 were also made and purified using HPLC, and SAXS data was analyzed for complexes. Based on our results we have proposed a fresh look at our perception of mAb-mediated neutralization. • Global structure analysis of tetravalent antibody CD4-IgG2 and its complexes with gp120 (dimeric to tetrameric complexes). • Designed biosimilars to CD4 IgG2 and currently comparing their neutralization efficacy with CD4 IgG2 and other neutralizing mAbs.
From 2015 to 2016, A novel mutation in CLCN5 associated with FSGS: Role of CLCN5 in podocyte and parietal epithelial cell biology , Glomerular diseases such as FSGS (Focal Segmental Glomerulosclerosis) are the third most frequent causes of end stage renal disease (ESRD)[1]. Although our understanding of the pathology of FSGS has significantly increased over the last decades, the underlying molecular mechanisms of FSGS are still not well understood. It has been increasingly recognized that mutations in genes that encode glomerular proteins particularly in visceral epithelial cells (podocytes) lead to development of FSGS[2]. These mutations are important not only because such patients should be spared from unnecessary toxic therapies but also because identification of mutations leads to discovery of important pathways of glomerular injury with potential for developing future targeted therapies. We have identified a novel variant (mutation, F521L) in “CLCN5 gene”, which codes for an endosomal chloride/hydrogen exchanger, responsible for the X-linked FSGS in a cohort of patients. The protein is known to be involved in
From 2012 to 2014, Vaccine design , Using KMP11, a Leishmania protein as a model system, we have shown that carrier protein influences immunodominance hierarchy which is an implication in vaccine design. Our result shows the presence of the epitope tag at the N and C terminal of native protein (KMP11) not only alters its global shape but also causes a difference in their immunogenicity.
From 2010 to 2011, DNA Protein Interaction , Molecular Docking Studies for HapR/DNA binding and confirming it by SAXS based study. Participated in visualizing the elusive open shape of G-actin in solution by SAXS data
Speciality
Structural Biology
Cell Biology
Molecular Biology
Nephrology
Virology
Biophysics
Biochemistry
Journal Articles
Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric. Ashish, Solanki AK, Boone CD, Krueger JK , (BBRC, 2009)
SAXS data analysis and modeling of tetravalent neutralizing antibody CD4-IgG2 -/+ HIV-1 gp120 revealed that first two gp120 bind to the same Fab arm. Rathore YS, Solanki AK, Dhoke RR, Ashish. , (BBRC, 2011)
Evidence on how a conserved glycine in the hinge region of Hapr regulates its DNA binding ability: lessons from a natural variant”. Dongre M, Singh NS, Dureja C, Peddada N, Solanki AK, Ashish, Raychaudhuri S.( JBC, 2011)
Visualizing the elusive open shape of G-actin in solution by SAXS data analysis Sagar A, Peddada N, Solanki AK, Choudhary Vikas, Garg, R., Ashish (BBRC May, 2013)
Carrier protein influences immunodominance hierarchy: implication in vaccine design. Moumita Ghosh, Solanki AK, Koushik Roy, Reema R. Dhoke, Ashish and Syamal Roy (VACCINE, JUNE 2013)
Global shape and ligand binding efficiency of the HIV-1 neutralizing antibodies differs from the ones which cannot neutralize. Solanki AK, Rathore YS, Badmalia MB, Dhoke RR, Nath SK, Nihalani N and Ashish (JBC, October, 2014)
Adriamycin susceptibility among C57BL/6 substrains. Ehtesham Arif, Solanki AK and Deepak Nihalani (Kidney International, 03/2016)
Structural analysis of the Myo1c and Neph1 complex provides insight into the intracellular movement of Neph1 Arif E, Sharma P, Solanki AK, Mallik L, Rathore YS, Twal WO, Nath SK, Gandhi D, Holzman LB, Ostap M, Ashish, Nihalani D (Mol Cell Biol., 2016)
Conference Papers
THE ASIAN PARTICLE TECHNOLOGY SYMPOSIUM (APT 2009)
“International conference on understanding and managing pathogenic microbes (UMPM)
Honors and Awards
Ben J. Lipps Research Fellowship, 2016
CSIR- UGC Senior Research Fellowship, 2011
CSIR- UGC Junior Research Fellowship, 2009
GATE-2008
Department of Biotechnology, Masters fellowship, 2007
ADDRESS
Science Publishing Group
548 FASHION AVENUE
NEW YORK, NY 10018
U.S.A.
Tel: (001)347-688-8931