Kishore Babu Bobbili

@allduniv.ac.in

Assistant Professor, Department of Chemistry
University of Allahabad

Kishore Babu Bobbili


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https://researchid.co/kishorehcu08

RESEARCH INTERESTS

Biophysical chemistry
13

Scopus Publications

395

Scholar Citations

9

Scholar h-index

9

Scholar i10-index

Scopus Publications

  • Structure and interactions of the phloem lectin (phloem protein 2) Cus17 from Cucumis sativus
    Kishore Babu Bobbili, Nukathoti Sivaji, Badma Priya, Kaza Suguna, Avadhesha Surolia
    Structure, 2023
  • Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
    Musti J. Swamy, Kishore Babu Bobbili, Saradamoni Mondal, Akkaladevi Narahari, Debparna Datta
    Phytochemistry, 2022
  • Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin
    Vaishali Narayanan, Kishore Babu Bobbili, Nukathoti Sivaji, Nisha G. Jayaprakash, Kaza Suguna, Avadhesha Surolia, Ashok Sekhar
    Biochemistry, 2022
    Lectins are sugar-binding proteins that have shown considerable promise as antiviral agents because of their ability to interact with envelope glycoproteins present on the surface of viruses such as HIV-1. However, their therapeutic potential has been compromised by their mitogenicity that stimulates uncontrolled division of T-lymphocytes. Horcolin, a member of the jacalin family of lectins, tightly binds the HIV-1 envelope glycoprotein gp120 and neutralizes HIV-1 particles but is nonmitogenic. In this report, we combine X-ray crystallography and NMR spectroscopy to obtain atomic-resolution insights into the structure of horcolin and the molecular basis for its carbohydrate recognition. Each protomer of the horcolin dimer adopts a canonical β-prism I fold with three Greek key motifs and carries two carbohydrate-binding sites. The carbohydrate molecule binds in a negatively charged pocket and is stabilized by backbone and side chain hydrogen bonds to conserved residues in the ligand-binding loop. NMR titrations reveal a two-site binding mode and equilibrium dissociation constants for the two binding sites determined from two-dimensional (2D) lineshape modeling are 4-fold different. Single-binding-site variants of horcolin confirm the dichotomy in binding sites and suggest that there is allosteric communication between the two sites. An analysis of the horcolin structure shows a network of hydrogen bonds linking the two carbohydrate-binding sites directly and through a secondary binding site, and this coupling between the two sites is expected to assume importance in the interaction of horcolin with high-mannose glycans found on viral envelope glycoproteins.
  • DSC and FCS Studies Reveal the Mechanism of Thermal and Chemical Unfolding of CIA17, a Polydisperse Oligomeric Protein fromCoccinia Indica
    Saradamoni Mondal, Kishore Babu Bobbili, Sumanta Paul, Musti J. Swamy
    Journal of Physical Chemistry B, 2021
    The mechanism of thermal and chemical unfolding of Coccinia indica agglutinin (CIA17), a chitooligosacharide-specific phloem exudate lectin, was investigated by biophysical approaches. DSC studies revealed that the unfolding thermogram of CIA17 consists of three components (Tm ∼ 98, 106, and 109 °C), which could be attributed to the dissociation of protein oligomers into constituent dimers, dissociation of the dimers into monomers, and unfolding of the monomers. Intrinsic fluorescence studies on the chemical denaturation by guanidinium thiocyanate and guanidinium chloride indicated the presence of two distinct steps in the unfolding pathway, which could be assigned to dissociation of the dimeric protein into monomers and unfolding of the monomers. Results of fluorescence correlation spectroscopic studies could be interpreted in terms of the following model: CIA17 forms oligomeric structures in a concentration dependent manner, with the protein existing as a monomer below 1 nM concentration but associating to form dimers at higher concentrations (KD ≈ 2.9 nM). The dimers associate to yield tetramers with a KD of ∼50 μM, which further associate to form higher oligomers with further increase in concentration. These results are consistent with the proposed role of CIA17 as a key player in the defense response of the plant against microbes and insects.
  • Chitooligosaccharide binding to CIA17 (Coccinia indica agglutinin). Thermodynamic characterization and formation of higher order complexes
    Kishore Babu Bobbili, Bipin Singh, Akkaladevi Narahari, Gopalakrishnan Bulusu, A. Surolia, Musti J. Swamy
    International Journal of Biological Macromolecules, 2019
  • Purification, chitooligosaccharide binding properties and thermal stability of CIA24, a new PP2-like phloem exudate lectin from ivy gourd (Coccinia indica)
    Kishore Babu Bobbili, Debparna Datta, Saradamoni Mondal, Sirilatha Polepalli, Gottfried Pohlentz, Michael Mormann, Musti J. Swamy
    International Journal of Biological Macromolecules, 2018
  • Coccinia indica agglutinin, a 17 kDa PP2 like phloem lectin: Affinity purification, primary structure and formation of self-assembled filaments
    Kishore Babu Bobbili, Gottfried Pohlentz, Akkaladevi Narahari, Kaushal Sharma, Avadhesha Surolia, Michael Mormann, Musti J. Swamy
    International Journal of Biological Macromolecules, 2018
  • Purification, physico-chemical characterization and thermodynamics of chitooligosaccharide binding to cucumber (Cucumis sativus) phloem lectin
    Pavan Kumar Nareddy, Kishore Babu Bobbili, Musti J. Swamy
    International Journal of Biological Macromolecules, 2017
  • Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses
    Jogi Madhuprakash, Kishore Babu Bobbili, Bruno M. Moerschbacher, Tej Pal Singh, Musti J. Swamy, Appa Rao Podile
    Scientific Reports, 2015
    Serratia proteamaculans chitinase-D (SpChiD) has a unique combination of hydrolytic and transglycosylation (TG) activities. The TG activity of SpChiD can be used for large-scale production of chito-oligosaccharides (CHOS). The multiple activities (hydrolytic and/or chitobiase activities and TG) of SpChiD appear to be strongly influenced by the substrate-binding cleft. Here, we report the unique property of SpChiD substrate-binding cleft, wherein, the residues Tyr28, Val35 and Thr36 control chitobiase activity and the residues Trp160 and Trp290 are crucial for TG activity. Mutants with reduced (V35G and T36G/F) or no (SpChiDΔ30-42 and Y28A) chitobiase activity produced higher amounts of the quantifiable even-chain TG product with degree of polymerization (DP)-6, indicating that the chitobiase and TG activities are inversely related. In addition to its unprecedented catalytic properties, unlike other chitinases, the single modular SpChiD showed dual unfolding transitions. Ligand-induced thermal stability studies with the catalytically inactive mutant of SpChiD (E153A) showed that the transition temperature increased upon binding of CHOS with DP2-6. Isothermal titration calorimetry experiments revealed the exceptionally high binding affinities for E153A to CHOS with DP2-6. These observations strongly support that the architecture of SpChiD substrate-binding cleft adopted to control chitobiase and TG activities, in addition to usual chitinase-mediated hydrolysis.
  • Structure of Chitosan determines its interactions with mucin
    B. Menchicchi, J. P. Fuenzalida, Kishore Babu Bobbili, A. Hensel, Musti J. Swamy, F. M. Goycoolea
    Biomacromolecules, 2014
    Synthetic and natural mucoadhesive biomaterials in optimized galenical formulations are potentially useful for the transmucosal delivery of active ingredients to improve their localized and prolonged effects. Chitosans (CS) have potent mucoadhesive characteristics, but the exact mechanisms underpinning such interactions at the molecular level and the role of the specific structural properties of CS remain elusive. In the present study we used a combination of microviscosimetry, zeta potential analysis, isothermal titration calorimetry (ITC) and fluorescence quenching to confirm that the soluble fraction of porcine stomach mucin interacts with CS in water or 0.1 M NaCl (at c < c*; relative viscosity, η(rel), ∼ 2.0 at pH 4.5 and 37 °C) via a heterotypic stoichiometric process significantly influenced by the degree of CS acetylation (DA). We propose that CS-mucin interactions are driven predominantly by electrostatic binding, supported by other forces (e.g., hydrogen bonds and hydrophobic association) and that the DA influences the overall conformation of CS and thus the nature of the resulting complexes. Although the conditions used in this model system are simpler than the typical in vivo environment, the resulting knowledge will enable the rational design of CS-based nanostructured materials for specific transmucosal drug delivery (e.g., for Helicobacter pylori stomach therapy).
  • Mutational analysis of the pumpkin (Cucurbita maxima) phloem exudate lectin, PP2 reveals Ser-104 is crucial for carbohydrate binding
    Kishore Babu Bobbili, Shyam Bandari, Kay Grobe, Musti J. Swamy
    Biochemical and Biophysical Research Communications, 2014
  • The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs
    Alok Sharma, Gottfried Pohlentz, Kishore Babu Bobbili, A. Arockia Jeyaprakash, Thyageshwar Chandran, Michael Mormann, Musti J. Swamy, M. Vijayan
    Acta Crystallographica Section D Biological Crystallography, 2013
  • Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation
    M. Kavitha, Kishore Babu Bobbili, Musti J. Swamy
    Biochimie, 2010

RECENT SCHOLAR PUBLICATIONS

  • Structure and interactions of the phloem lectin (phloem protein 2) Cus17 from Cucumis sativus
    KB Bobbili, N Sivaji, B Priya, K Suguna, A Surolia
    Structure 31 (4), 464-479. e5 , 2023
    2023.0
    Citations: 17
  • Cucurbitaceae phloem exudate lectins: purification, molecular characterization and carbohydrate binding characteristics
    MJ Swamy, KB Bobbili, S Mondal, A Narahari, D Datta
    Phytochemistry 201, 113251 , 2022
    2022.0
    Citations: 9
  • Structure and carbohydrate recognition by the nonmitogenic lectin horcolin
    V Narayanan, KB Bobbili, N Sivaji, NG Jayaprakash, K Suguna, A Surolia, ...
    Biochemistry 61 (6), 464-478 , 2022
    2022.0
    Citations: 5
  • Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin
    KB Bobbili
    Biochemistry , 2022
    2022.0
  • DSC and FCS Studies Reveal the Mechanism of Thermal and Chemical Unfolding of CIA17, a Polydisperse Oligomeric Protein from Coccinia Indica
    S Mondal, KB Bobbili, S Paul, MJ Swamy
    The Journal of Physical Chemistry B 125 (26), 7117-7127 , 2021
    2021.0
    Citations: 4
  • Chitooligosaccharide binding to CIA17 (Coccinia indica agglutinin). Thermodynamic characterization and formation of higher order complexes
    KB Bobbili, B Singh, A Narahari, G Bulusu, A Surolia, MJ Swamy
    International Journal of Biological Macromolecules 137, 774-782 , 2019
    2019.0
    Citations: 9
  • Purification, chitooligosaccharide binding properties and thermal stability of CIA24, a new PP2-like phloem exudate lectin from ivy gourd (Coccinia indica)
    KB Bobbili, D Datta, S Mondal, S Polepalli, G Pohlentz, M Mormann, ...
    International journal of biological macromolecules 110, 588-597 , 2018
    2018.0
    Citations: 12
  • Coccinia indica agglutinin, a 17 kDa PP2 like phloem lectin: affinity purification, primary structure and formation of self-assembled filaments
    KB Bobbili, G Pohlentz, A Narahari, K Sharma, A Surolia, M Mormann, ...
    International journal of biological macromolecules 108, 1227-1236 , 2018
    2018.0
    Citations: 23
  • Purification, physico-chemical characterization and thermodynamics of chitooligosaccharide binding to cucumber (Cucumis sativus) phloem lectin
    PK Nareddy, KB Bobbili, MJ Swamy
    International journal of biological macromolecules 95, 910-919 , 2017
    2017.0
    Citations: 26
  • Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical …
    J Madhuprakash, KB Bobbili, BM Moerschbacher, TP Singh, MJ Swamy, ...
    Scientific Reports 5 (1), 15657 , 2015
    2015.0
    Citations: 27
  • Structure of chitosan determines its interactions with mucin
    B Menchicchi, JP Fuenzalida, KB Bobbili, A Hensel, MJ Swamy, ...
    Biomacromolecules 15 (10), 3550-3558 , 2014
    2014.0
    Citations: 187
  • Mutational analysis of the pumpkin (Cucurbita maxima) phloem exudate lectin, PP2 reveals Ser-104 is crucial for carbohydrate binding
    KB Bobbili, S Bandari, K Grobe, MJ Swamy
    Biochemical and biophysical research communications 450 (1), 622-627 , 2014
    2014.0
    Citations: 13
  • Mucin-polysaccharides interactions: In search of a nanobioplatform for Helicobacter pylori therapy
    B Menchicchi, JPF Werner, KB Bobbili, A Hensel, MJ Swamy, ...
    Planta Medica 79 (13), PN63 , 2013
    2013.0
    Citations: 1
  • The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs
    A Sharma, G Pohlentz, KB Bobbili, AA Jeyaprakash, T Chandran, ...
    Biological Crystallography 69 (8), 1493-1503 , 2013
    2013.0
    Citations: 29
  • Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation
    M Kavitha, KB Bobbili, MJ Swamy
    Biochimie 92 (1), 58-64 , 2010
    2010.0
    Citations: 33
  • Full wwPDB X-ray Structure Validation Report i○
    F Alaleona, A Ilari, E Chiancone, A Battistoni, P Petrarca

MOST CITED SCHOLAR PUBLICATIONS

  • Structure of chitosan determines its interactions with mucin
    B Menchicchi, JP Fuenzalida, KB Bobbili, A Hensel, MJ Swamy, ...
    Biomacromolecules 15 (10), 3550-3558 , 2014
    2014.0
    Citations: 187
  • Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation
    M Kavitha, KB Bobbili, MJ Swamy
    Biochimie 92 (1), 58-64 , 2010
    2010.0
    Citations: 33
  • The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs
    A Sharma, G Pohlentz, KB Bobbili, AA Jeyaprakash, T Chandran, ...
    Biological Crystallography 69 (8), 1493-1503 , 2013
    2013.0
    Citations: 29
  • Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical …
    J Madhuprakash, KB Bobbili, BM Moerschbacher, TP Singh, MJ Swamy, ...
    Scientific Reports 5 (1), 15657 , 2015
    2015.0
    Citations: 27
  • Purification, physico-chemical characterization and thermodynamics of chitooligosaccharide binding to cucumber (Cucumis sativus) phloem lectin
    PK Nareddy, KB Bobbili, MJ Swamy
    International journal of biological macromolecules 95, 910-919 , 2017
    2017.0
    Citations: 26
  • Coccinia indica agglutinin, a 17 kDa PP2 like phloem lectin: affinity purification, primary structure and formation of self-assembled filaments
    KB Bobbili, G Pohlentz, A Narahari, K Sharma, A Surolia, M Mormann, ...
    International journal of biological macromolecules 108, 1227-1236 , 2018
    2018.0
    Citations: 23
  • Structure and interactions of the phloem lectin (phloem protein 2) Cus17 from Cucumis sativus
    KB Bobbili, N Sivaji, B Priya, K Suguna, A Surolia
    Structure 31 (4), 464-479. e5 , 2023
    2023.0
    Citations: 17
  • Mutational analysis of the pumpkin (Cucurbita maxima) phloem exudate lectin, PP2 reveals Ser-104 is crucial for carbohydrate binding
    KB Bobbili, S Bandari, K Grobe, MJ Swamy
    Biochemical and biophysical research communications 450 (1), 622-627 , 2014
    2014.0
    Citations: 13
  • Purification, chitooligosaccharide binding properties and thermal stability of CIA24, a new PP2-like phloem exudate lectin from ivy gourd (Coccinia indica)
    KB Bobbili, D Datta, S Mondal, S Polepalli, G Pohlentz, M Mormann, ...
    International journal of biological macromolecules 110, 588-597 , 2018
    2018.0
    Citations: 12
  • Cucurbitaceae phloem exudate lectins: purification, molecular characterization and carbohydrate binding characteristics
    MJ Swamy, KB Bobbili, S Mondal, A Narahari, D Datta
    Phytochemistry 201, 113251 , 2022
    2022.0
    Citations: 9
  • Chitooligosaccharide binding to CIA17 (Coccinia indica agglutinin). Thermodynamic characterization and formation of higher order complexes
    KB Bobbili, B Singh, A Narahari, G Bulusu, A Surolia, MJ Swamy
    International Journal of Biological Macromolecules 137, 774-782 , 2019
    2019.0
    Citations: 9
  • Structure and carbohydrate recognition by the nonmitogenic lectin horcolin
    V Narayanan, KB Bobbili, N Sivaji, NG Jayaprakash, K Suguna, A Surolia, ...
    Biochemistry 61 (6), 464-478 , 2022
    2022.0
    Citations: 5
  • DSC and FCS Studies Reveal the Mechanism of Thermal and Chemical Unfolding of CIA17, a Polydisperse Oligomeric Protein from Coccinia Indica
    S Mondal, KB Bobbili, S Paul, MJ Swamy
    The Journal of Physical Chemistry B 125 (26), 7117-7127 , 2021
    2021.0
    Citations: 4
  • Mucin-polysaccharides interactions: In search of a nanobioplatform for Helicobacter pylori therapy
    B Menchicchi, JPF Werner, KB Bobbili, A Hensel, MJ Swamy, ...
    Planta Medica 79 (13), PN63 , 2013
    2013.0
    Citations: 1
  • Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin
    KB Bobbili
    Biochemistry , 2022
    2022.0
  • Full wwPDB X-ray Structure Validation Report i○
    F Alaleona, A Ilari, E Chiancone, A Battistoni, P Petrarca