Abstract
F-type lectins are phylogenetically widespread albeit selectively distributed lectins with an L-fucose-binding sequence motif and an F-type lectin fold. Several F-type lectins from fishes have been extensively studied, and structural information is available for F-type lectin domains from fish and bacterial proteins. F-type lectins have been demonstrated to be involved in self−/nonself-recognition and therefore have an important role in pathogen defense in many metazoan animals. F-type lectin domains also have been implicated in functions related to fertilization, protoplast regeneration, and bacterial virulence. We have recently analyzed and reported the taxonomic spread, phylogenetic distribution, architectural contexts, and sequence characteristics of prokaryotic and eukaryotic F-type lectin domains. Interestingly, while eukaryotic F-type lectin domains were frequently present as stand-alone domains, bacterial F-type lectin domains were mostly found co-occurring with enzymatic or nonenzymatic domains in diverse domain architectures, suggesting that the F-type lectin domain might be involved in targeting enzyme activities or directing other biological functions to distinct glycosylated niches in bacteria. We and others have probed the fine oligosaccharide-binding specificity of several F-type lectin domains. The currently available wealth of sequence, structural, and biochemical information about F-type lectin domains provides opportunities for the generation of designer lectins with improved binding strength and altered binding specificities. We discuss the prevalence, provenance, properties, peculiarities, and potential of F-type lectin domains for future applications in this review.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Arivalagan J, Marie B, Sleight VA, Clark MS, Berland S, Marie A (2016) Shell matrix proteins of the clam, Mya truncata: roles beyond shell formation through proteomic study. Mar Genomics 27:69–74. https://doi.org/10.1016/j.margen.2016.03.005
Baldus SE, Thiele J, Park YO, Hanisch FG, Bara J, Fischer R (1996) Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I). Glycoconj J 13(4):585–590
Bianchet MA, Odom EW, Vasta GR, Amzel LM (2002) A novel fucose recognition fold involved in innate immunity. Nat Struct Biol 9(8):628–634. https://doi.org/10.1038/nsb817
Bianchet MA, Odom EW, Vasta GR, Amzel LM (2010) Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis). J Mol Biol 401(2):239–252. https://doi.org/10.1016/j.jmb.2010.06.018
Bishnoi R, Khatri I, Subramanian S, Ramya TN (2015) Prevalence of the F-type lectin domain. Glycobiology 25(8):888–901. https://doi.org/10.1093/glycob/cwv029
Bishnoi R, Mahajan S, Ramya TNC (2018) An F-type lectin domain directs the activity of Streptosporangium roseum alpha-L-fucosidase. Glycobiology 28(11):860–875
Boraston AB, Wang D, Burke RD (2006) Blood group antigen recognition by a Streptococcus pneumoniae virulence factor. J Biol Chem 281(46):35263–35271. https://doi.org/10.1074/jbc.M607620200
Cammarata M, Vazzana M, Chinnici C, Parrinello N (2001) A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax. BBA-Gen Subjects 1528(2-3):196–202
Cammarata M, Benenati G, Odom EW, Salerno G, Vizzini A, Vasta GR, Parrinello N (2007) Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum. Biochim Biophys Acta 1770(1):150–155. https://doi.org/10.1016/j.bbagen.2006.09.015
Cammarata M, Salerno G, Parisi MG, Benenati G, Vizzini A, Vasta GR, Parrinello N (2012) Primary structure and opsonic activity of an F-lectin from serum of the gilt head bream Sparus aurata (Pisces, Sparidae). Ital J Zool 79(1):34–43. https://doi.org/10.1080/11250003.2011.596167
Cassels FJ, Odom EW, Vasta GR (1994) Hemolymph lectins of the blue crab, Callinectes sapidus, recognize selected serotypes of its pathogen Vibrio parahaemolyticus. Ann N Y Acad Sci 712:324–326
Chen J, Xiao S, Yu Z (2011) F-type lectin involved in defense against bacterial infection in the pearl oyster (Pinctada martensii). Fish Shellfish Immunol 30(2):750–754. https://doi.org/10.1016/j.fsi.2010.12.025
Cho SY, Kwon J, Vaidya B, Kim JO, Lee S, Jeong EH, Baik KS, Choi JS, Bae HJ, Oh MJ, Kim D (2014) Modulation of proteome expression by F-type lectin during viral hemorrhagic septicemia virus infection in fathead minnow cells. Fish Shellfish Immunol 39(2):464–474. https://doi.org/10.1016/j.fsi.2014.05.042
Danguy A, Kiss R, Pasteels JL (1988) Lectins in histochemistry. A survey. Biol Struct Morphog 1(3):93–106
Farrand S, Hotze E, Friese P, Hollingshead SK, Smith DF, Cummings RD, Dale GL, Tweten RK (2008) Characterization of a streptococcal cholesterol-dependent cytolysin with a Lewis y and b specific lectin domain. Biochemistry 47(27):7097–7107. https://doi.org/10.1021/Bi8005835
Feil SC, Lawrence S, Mulhern TD, Holien JK, Hotze EM, Farrand S, Tweten RK, Parker MW (2012) Structure of the lectin regulatory domain of the cholesterol-dependent Cytolysin Lectinolysin reveals the basis for its Lewis antigen specificity. Structure 20(2):248–258. https://doi.org/10.1016/j.str.2011.11.017
Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014) Pfam: the protein families database. Nucleic Acids Res 42(Database issue):D222–D230. https://doi.org/10.1093/nar/gkt1223
Fleming RI, Mackenzie CD, Cooper A, Kennedy MW (2009) Foam nest components of the tungara frog: a cocktail of proteins conferring physical and biological resilience. Proc Biol Sci 276(1663):1787–1795. https://doi.org/10.1098/rspb.2008.1939
Gorbushin AM, Borisova EA (2015) Lectin-like molecules in transcriptome of Littorina littorea hemocytes. Dev Comp Immunol 48(1):210–220. https://doi.org/10.1016/j.dci.2014.10.007
Gouet P, Robert X, Courcelle E (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31(13):3320–3323
Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233(1):123–138. https://doi.org/10.1006/jmbi.1993.1489
Honda S, Kashiwagi M, Miyamoto K, Takei Y, Hirose S (2000) Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins. J Biol Chem 275(42):33151–33157. https://doi.org/10.1074/jbc.M002337200
Jaroszewski L, Rychlewski L, Li Z, Li W, Godzik A (2005) FFAS03: a server for profile-profile sequence alignments. Nucleic Acids Res 33(Web Server issue):W284–W288. https://doi.org/10.1093/nar/gki418
Judd JW, Issitt PD (1980) The role of lectins in blood group serology. CRC Crit Rev Clin Lab Sci 12(3):171–214
Kim GH, Klochkova TA, Yoon KS, Song YS, Lee KP (2006) Purification and characterization of a lectin, bryohealin, involved in the protoplast formation of a marine green alga Bryopsis plumosa (Chlorophyta). J Phycol 42(1):86–95. https://doi.org/10.1111/j.1529-8817.2005.00162.x
Liu W, Xie Y, Ma J, Luo X, Nie P, Zuo Z, Lahrmann U, Zhao Q, Zheng Y, Zhao Y, Xue Y, Ren J (2015) IBS: an illustrator for the presentation and visualization of biological sequences. Bioinformatics 31(20):3359–3361. https://doi.org/10.1093/bioinformatics/btv362
Mahajan S, Khairnar A, Bishnoi R, Ramya TNC (2017) Microbial F-type lectin domains with affinity for blood group antigens. Biochem Biophys Res Commun 491(3):708–713. https://doi.org/10.1016/j.bbrc.2017.07.125
Mahajan S, Ramya TNC (2018) Nature-inspired engineering of an F-type lectin for increased binding strength. Glycobiology:cwy082
Maki M, Renkonen R (2004) Biosynthesis of 6-deoxyhexose glycans in bacteria. Glycobiology 14(3):1R–15R. https://doi.org/10.1093/glycob/cwh040
Multerer KA, Smith LC (2004) Two cDNAs from the purple sea urchin, Strongylocentrotus purpuratus, encoding mosaic proteins with domains found in factor H, factor I, and complement components C6 and C7. Immunogenetics 56(2):89–106. https://doi.org/10.1007/s00251-004-0665-2
Notredame C, Higgins DG, Heringa J (2000) T-coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302(1):205–217. https://doi.org/10.1006/jmbi.2000.4042
Odom EW, Vasta GR (2006) Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis). J Biol Chem 281(3):1698–1713. https://doi.org/10.1074/jbc.M507652200
Riely BK, Ane JM, Penmetsa RV, Cook DR (2004) Genetic and genomic analysis in model legumes bring Nod-factor signaling to center stage. Curr Opin Plant Biol 7(4):408–413. https://doi.org/10.1016/j.pbi.2004.04.005
Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5(4):725–738. https://doi.org/10.1038/nprot.2010.5
Saito T, Hatada M, Iwanaga S, Kawabata S (1997) A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem 272(49):30703–30708
Salerno G, Parisi MG, Parrinello D, Benenati G, Vizzini A, Vazzana M, Vasta GR, Cammarata M (2009) F-type lectin from the sea bass (Dicentrarchus labrax): purification, cDNA cloning, tissue expression and localization, and opsonic activity. Fish Shellfish Immun 27(2):143–153. https://doi.org/10.1016/j.fsi.2009.01.004
Samuel G, Reeves P (2003) Biosynthesis of O-antigens: genes and pathways involved in nucleotide sugar precursor synthesis and O-antigen assembly. Carbohydr Res 338(23):2503–2519. https://doi.org/10.1016/j.carres.2003.07.009
Springer GF, Desai PR (1970) The immunochemical requirements for specific activity and the physiochemical properties of eel anti-human blood-group H(O) 7 S globulin. Vox Sang 18(6):551–554
Springer SA, Moy GW, Friend DS, Swanson WJ, Vacquier VD (2008) Oyster sperm bindin is a combinatorial fucose lectin with remarkable intra-species diversity. Int J Dev Biol 52(5-6):759–768. https://doi.org/10.1387/ijdb.082581ss
Takaichi S, Maoka T, Masamoto K (2001) Myxoxanthophyll in Synechocystis sp PCC 6803 is myxol 2′-dimethyl-fucoside, (3R,2′S)-myxol 2′-(2,4-di-O-methyl-alpha-L-fucoside), not rhamnoside. Plant Cell Physiol 42(7):756–762. https://doi.org/10.1093/Pcp/Pce098
Vasta GR, Ahmed H, Odom EW (2004) Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Curr Opin Struct Biol 14(5):617–630. https://doi.org/10.1016/j.sbi.2004.09.008
Vasta GR, Odom EW, Bianchet MA, Amzel LM, Saito K, Ahmed H (2008) F-type lectins: a new family of recognition factors. In: Vasta GR, Ahmed H (eds) Animal lectins: a functional view. CRC Press, London
Vasta GR, Amzel LM, Bianchet MA, Cammarata M, Feng C, Saito K (2017) F-type lectins: a highly diversified family of Fucose-binding proteins with a unique sequence motif and structural fold, involved in self/non-self-recognition. Front Immunol 8:1648. https://doi.org/10.3389/fimmu.2017.01648
Wagner M (1988) Light and electron microscopic lectin histochemistry using fluorochromes and ferritin as labels. Acta Histochem Suppl 36:115–123
Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y (2015) The I-TASSER suite: protein structure and function prediction. Nat Methods 12(1):7–8. https://doi.org/10.1038/nmeth.3213
Yoon KS, Lee KP, Klochkova TA, Kim GH (2008) Molecular characterization of the lectin, bryohealin, involved in protoplast regeneration of the marine alga Bryopsis plumosa (Chlorophyta). J Phycol 44(1):103–112. https://doi.org/10.1111/j.1529-8817.2007.00457.x
Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. https://doi.org/10.1186/1471-2105-9-40
Acknowledgments
The authors’ research described in this review was enabled by a research grant from the Department of Science and Technology, Government of India, to RTNC (FAST-TRACK grant no. SR/FT/LS-87/2012 to RTNC) and infrastructure and research facilities provided by the CSIR-Institute of Microbial Technology, Chandigarh (manuscript number 05/2018). SM is a DBT Senior Research Fellow.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Mahajan, S., Ramya, T.N.C. (2018). F-type Lectin Domains: Provenance, Prevalence, Properties, Peculiarities, and Potential. In: Chattopadhyay, K., Basu, S. (eds) Biochemical and Biophysical Roles of Cell Surface Molecules. Advances in Experimental Medicine and Biology, vol 1112. Springer, Singapore. https://doi.org/10.1007/978-981-13-3065-0_24
Download citation
DOI: https://doi.org/10.1007/978-981-13-3065-0_24
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-13-3064-3
Online ISBN: 978-981-13-3065-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)