02294nas a2200241 4500008004100000022001400041245009300055210006900148260006700217300001000284490000700294520147800301653001701779653002001796653001401816653001101830653001201841653001401853100001601867700001701883700002601900856012601926 2007 eng d a1521-654300aChemical, thermal and pH-induced equilibrium unfolding studies of fusarium solani lectin0 aChemical thermal and pHinduced equilibrium unfolding studies of  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcDEC a34-430 v593 a

The effect of urea, guanidine thiocyanate, temperature and pH was studied on the conformational stability of Fusarium solani lectin. Equilibrium unfolding with chemical denaturants showed that the lectin was least stable at pH 12 and maximally stable at pH 8.0 near its pI ( 8.7). Guanidine thiocyanate ( the concentration of denaturant at which the protein is half folded, D-1/2 = 0.49 M at pH 12) was found to be an eight times stronger denaturant than urea (D-1/2 = 3.88 M at pH 12). The unfolding curves obtained with fluorescence and CD measurements showed good agreement indicating a monophasic nature of unfolding and excluded the possibility of formation of any stable intermediate. The effect of pH on the lectin was found to be unusual as at acidic pH, the lectin showed a flexible tertiary structure with pronounced secondary structure, and retained its hemagglutinating activity. On the other hand, the lectin did not show any loss of conformation or activity upto 70 degrees C for 15 min. Moreover, thermal denaturation did not result in the aggregation or precipitation of the protein even at high temperatures. Thermal denaturation was also carried out in the presence of a low concentration of guanidine thiocyanate. Change in the enthalpy of transition (Delta H-m) varied linearly with transition temperature (T-m), which indicated that the heat capacity (Delta C-p =3.95 kJ (.) mol(-1) (.) K-1) of the lectin remained constant during the unfolding.

10aDenaturation10aFusarium solani10aguanidine10aLectin10athermal10aUnfolding1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/chemical-thermal-and-ph-induced-equilibrium-unfolding-studies-fusarium-solani-lectin-001832nas a2200229 4500008004100000022001400041245012200055210006900177260006800246300001200314490000700326520101100333653002201344653001201366653001101378653000801389100001701397700001601414700001701430700002601447856012901473 2007 eng d a1521-654300aComplex carbohydrate specificity of lectin from fruiting body of ganoderma lucidum. a surface plasmon resonance study0 aComplex carbohydrate specificity of lectin from fruiting body of a111 RIVER ST, HOBOKEN, NJ 07030 USAbJOHN WILEY & SONS INCcJAN a758-7640 v593 a

The thermodynamics and kinetics of binding of glycans and glycoproteins to Ganoderma lucidum lectin was studied using surface plasmon resonance. The lectin showed highest affinity for asialo triantennary N glycan (Ka = 3.52 x 10(5)) among the glycans tested. There was a several fold increase in affinity for glycoproteins compared to their corresponding glycans and coincident increase in contribution from enthalpy (Delta H), suggesting the involvement of hydrogen bonding in the interaction as well as involvement of protein-protein interactions. Increased affinity also showed increase in unfavorable negative binding entropy (Delta S) which was compensated with higher enthalpy. The glycoproteins showed faster association rates (k(1)) and the activation energy (E-1(double dagger)) in the association process was much lower for the glycoproteins than glycans, resulting in their faster associations. These observations elaborate the role of protein matrix in lectin-glycoconjugate interaction.

10aganoderma lucidum10aglycans10aLectin10aSPR1 aThakur, Atul1 aPal, Lakhan1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/complex-carbohydrate-specificity-lectin-fruiting-body-ganoderma-lucidum-surface-plasmon-001805nas a2200241 4500008004100000022001400041245012200055210006900177260007900246300001200325490000800337520092300345653002201268653002001290653001101310653001701321653000801338653002901346100001601375700001701391700002601408856012901434 2007 eng d a0003-986100aPurification and characterization of a lectin from endophytic fungus fusarium solani having complex sugar specificity0 aPurification and characterization of a lectin from endophytic fu a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcJAN a243-2510 v4573 a

A lectin from the mycelial extract of an endophytic strain of Fusarium solani was purified. Its hemagglutinating activity was inhibited by glycoproteins possessing N-linked as well as O-linked glycans. The thermodynamics and kinetics of binding of glycans and glycoproteins to F. solani lectin Was Studied using SUH ace plasmon resonance. The lectin showed high affinity for asialofetuin, asia-lofibrinogen, asialofibrinogen, and thyroglobulin: and comparatively low affinity for mucin, fetuin, fibrinogen, and holotransferrin. Glycoproteins showed glycans with significant contribution from enthalpy and positive entropy, suggesting several fold higher affinity than their corresponding g the involvement of non-polar protein-protein interaction. Moreover, the higher affinity of the glycoproteins was due to their faster association rates and low activation energy. (c) 2006 Elsevier Inc. All rights reserved.

10aendophytic fungus10aFusarium solani10aLectin10aPurification10aSPR10aThermodynamic properties1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/purification-and-characterization-lectin-endophytic-fungus-fusarium-solani-having-complex01956nas a2200229 4500008004100000022001400041245015200055210006900207260008900276300001200365490000700377520103600384653003001420653002201450653001101472653002401483653002901507100002301536700001801559700002601577856012301603 2008 eng d a1050-464800aPurification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)0 aPurification and characterization of a Tantigen specific lectin  a24-28 OVAL RD, LONDON NW1 7DX, ENGLANDbACADEMIC PRESS LTD ELSEVIER SCIENCE LTDcAPR a450-4580 v243 a

A novel lectin was purified from the coelomic fluid of the sea cucumber Holothuria scabra (HSL), subjected to bacterial challenge. HSL is a monomeric glycoprotein of molecular mass 182 kDa. The lectin is highly thermostable as it retains full activity for 1 h at 80 degrees C. Further, the hemagglutination activity of HSL is unaffected by pH in the range 2-11. Unlike other lectins purified from marine invertebrates, the hemagglutination activity of HSL does not require any divalent metal ions. The affinity profile of HSL was studied by a combination of hemagglutination inhibition and fluorescence spectroscopy. HSL binds to desialylated glycoproteins, Me alpha Gal, T-antigen and T (alpha-ser)-antigen with a distinction between beta 1-4 and beta 1-3 linkages. Me alpha-T-antigen was a potent ligand having highest affinity (K-a 8.32 x 10(7) M-1). Monosaccharide binding is enthalphically driven while disaccharide binding involves both entropic and enthalpic contributions. (c) 2008 Elsevier Ltd. All rights reserved.

10aFluorescence spectroscopy10aHolothuria scabra10aLectin10amarine invertebrate10aThermodynamic properties1 aGowda, Nagaraj, M.1 aGoswami, Usha1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/purification-and-characterization-t-antigen-specific-lectin-coelomic-fluid-marine-001836nas a2200241 4500008004100000022001400041245017800055210006900233260009500302300001200397490000700409520087500416653001801291653002701309653001901336653002201355653001101377653001701388100002301405700001801428700002601446856012201472 2008 eng d a0022-201100aT-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): possible involvement in differential recognition of bacteria0 aTantigen binding lectin with antibacterial activity from marine  a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcOCT a141-1450 v993 a

In invertebrates, cellular and humoral components are evolved to maintain their body immunity and integrity. Both these factors respond to different antigens such as microorganisms, vertebrate erythrocytes and foreign proteins. In this article, we report a study of a lectin (HSL) involved in immune response in the echinoderm, sea Cucumber (Holothuria scabra). Correlative studies indicate that the expression of this defensive lectin is induced by bacterial challenge, wherein cell wall glycoconjugates of bacteria are involved in lectin induction. HSL showed strong broad spectrum antibacterial activity against both gram-positive and gram-negative bacteria. Under in vitro conditions, purified HSL mediate agglutination of the test bacteria, there by indicating a possible mode of action in physiological situation. (c) 2008 Elsevier Inc. All rights reserved.

10aagglutination10aantibacterial activity10acoelomic fluid10aHolothuria scabra10aLectin10asea cucumber1 aGowda, Nagaraj, M.1 aGoswami, Usha1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/t-antigen-binding-lectin-antibacterial-activity-marine-invertebrate-sea-cucumber-002268nas a2200241 4500008004100000022001400041245014300055210006900198260007500267300001200342490000700354520137800361653002601739653001701765653001301782653001101795653001401806653001801820100001601838700001701854700002601871856012901897 2010 eng d a1053-050900aSteady state and time resolved fluorescence quenching and chemical modification studies of a lectin from endophytic fungus fusarium solani0 aSteady state and time resolved fluorescence quenching and chemic a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScJAN a305-3130 v203 a

The solute quenching studies of a lectin from endophytic fungus Fusarium solani were carried out using different quenchers such as acrylamide, succinimide, potassium iodide and cesium chloride. The lectin showed emission maximum at 348 nm indicating relative exposure of tryptophan. The quenchable fraction of the fluorophore was 100% with acrylamide, whereas it was only 50% with succinimide. The ionic quenchers iodide and cesium showed opposite effects at different pH. In the case of cesium, raising the pH resulted in increased quenching and accessibility of typtophan residue, while the iodide showed just opposite effect. These studies showed that the single tryptophan residue of the lectin (per monomer) is relatively exposed, and might be in the vicinity of positively charged amino acid residues. Various amino acids of the F. solani lectin were modified using different reagents to obtain information about the hemagglutinating site. The chemical modification studies suggested tyrosine residues can be modified using N-acetylimidazole, which results in complete loss of hemagglutination activity of the lectin. Kinetics of chemical modification suggested involvement of only 2 tyrosine residues. Modification of arginine, cysteine, histidine, lysine, aspartate, glutamate and tryptophan did not result in loss of hemagglutinating activity of the lectin.

10aChemical modification10afluorescence10aFusarium10aLectin10aQuenching10aTime-resolved1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/steady-state-and-time-resolved-fluorescence-quenching-and-chemical-modification-studies-002404nas a2200229 4500008004100000022001400041245016300055210006900218260007500287300001400362490000700376520146300383653002201846653002101868653001101889653004301900653002901943100002301972700002501995700002602020856012802046 2013 eng d a1053-050900aKinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: a fluorescence and surface plasmon resonance spectroscopic study0 aKinetics and thermodynamics of glycans and glycoproteins binding a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScNOV a1147-11550 v233 a

Holothuria scabra produces a monomeric lectin (HSL) of 182 kDa. HSL showed strong antibacterial activity and induced bacterial agglutination under in vitro conditions, indicating its role in animals' innate immune responses. Very few lectins have been reported from echinoderms and none of these lectins have been explored in detail for their sugar-binding kinetics. Affinity, kinetics and thermodynamic analysis of glycans and glycoproteins binding to HSL were studied by fluorescence and surface plasmon resonance spectroscopy. Lectin binds with higher affinity to O-linked than N-linked asialo glycans, and the affinities were relatively higher than that for sialated glycans and glycoproteins. T-antigen alpha-methyl glycoside was the most potent ligand having the highest affinity (Ka 8.32 x10(7) M-1). Thermodynamic and kinetic analysis indicated that the binding of galactosyl Tn-antigen and asialo glycans is accompanied by an enthalpic contribution in addition to higher association rate coupled by low activation energy for the association process. Presence of sialic acid or protein matrix inhibits binding. Higher affinity of HSL for O-glycans than N-glycans had biological implications; since HSL specifically recognizes bacteria, which have mucin or O-glycan cognate on their cell surfaces and play a major role in animal innate immunity. Since, HSL had higher affinity to T-antigen, makes it a useful tool for cancer diagnostic purpose.

10aHolothuria scabra10aKinetic analysis10aLectin10aSurface plasmon resonance spectroscopy10aThermodynamic properties1 aGowda, Nagaraj, M.1 aGaikwad, Sushama, M.1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/kinetics-and-thermodynamics-glycans-and-glycoproteins-binding-holothuria-scabra-lectin-002220nas a2200241 4500008004100000022001400041245012000055210006900175260000900244300001200253490000800265520138800273653001701661653001901678653001101697653001901708653002301727653002401750100002801774700002101802700002501823856013001848 2019 eng d a0003-986100aInvestigation of structural and saccharide binding transitions of Bauhinia purpurea and Wisteria floribunda lectins0 aInvestigation of structural and saccharide binding transitions o cFEB  a134-1420 v6623 a

Two novel medicinally important legume lectins from Bauhinia purpurea (BPL) and Wisteria floribunda (WFL) possessing extended sugar binding site were investigated for functional and conformational transitions using biochemical and biophysical techniques as well as bioinformatical tools. Homology model of BPL was constructed using the Schrodinger suite and docked with N-acetyl galactosamine and T-antigen disaccharide (Gal beta 1-3GalNAc alpha O-Me). The longer loop D in the structure of WFL compared to that in BPL was found to be responsible for its specificity to LacdiNac (beta-D-GalNAc-[1 -> 4]-DGlcNAc) over Gal beta 1-3GalNAc. BPL remained functionally stable up to 40 degrees C whereas WFL remained stable upto 70 degrees C indicating the strength of the sugar binding site geometry. Both the lectins showed intense but non-specific secondary structure in the range of 65-90 degrees C. WFL showed rapid aggregation above 80 degrees C as indicated by light scattering intensity. The lectins showed simultaneous dissociation and multistate unfolding in the vicinity of GdnHCl. At pH 1.0, both the lectins exhibited molten globule like structures, which were characterized further and were found to respond in a different way towards denaturants. The results have provided valuable insights into the molecular basis of the activity and stability of the two lectins.

10aConformation10aHomology model10aLectin10aMolten globule10asaccharide binding10aThermal aggregation1 aAgrawal, Sanskruthi, B.1 aGhosh, Deepanjan1 aGaikwad, Sushama, M. uhttps://library.ncl.res.in/content/investigation-structural-and-saccharide-binding-transitions-bauhinia-purpurea-and-wisteria