F-type Lectin Domains: Provenance, Prevalence, Properties, Peculiarities, and Potential

  • Sonal Mahajan
  • T. N. C. RamyaEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1112)


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.


F-type lectin domain L-fucose Motif Domain architectures Structural features 



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.


  1. 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. CrossRefPubMedGoogle Scholar
  2. 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):585–590CrossRefGoogle Scholar
  3. 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. CrossRefPubMedGoogle Scholar
  4. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  5. Bishnoi R, Khatri I, Subramanian S, Ramya TN (2015) Prevalence of the F-type lectin domain. Glycobiology 25(8):888–901. CrossRefPubMedGoogle Scholar
  6. Bishnoi R, Mahajan S, Ramya TNC (2018) An F-type lectin domain directs the activity of Streptosporangium roseum alpha-L-fucosidase. Glycobiology 28(11):860–875CrossRefGoogle Scholar
  7. Boraston AB, Wang D, Burke RD (2006) Blood group antigen recognition by a Streptococcus pneumoniae virulence factor. J Biol Chem 281(46):35263–35271. CrossRefPubMedGoogle Scholar
  8. 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):196–202CrossRefGoogle Scholar
  9. 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. CrossRefPubMedGoogle Scholar
  10. 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. CrossRefGoogle Scholar
  11. 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 712:324–326CrossRefGoogle Scholar
  12. 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. CrossRefPubMedGoogle Scholar
  13. 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. CrossRefPubMedGoogle Scholar
  14. Danguy A, Kiss R, Pasteels JL (1988) Lectins in histochemistry. A survey. Biol Struct Morphog 1(3):93–106PubMedGoogle Scholar
  15. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  16. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  17. 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. CrossRefGoogle Scholar
  18. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  19. Gorbushin AM, Borisova EA (2015) Lectin-like molecules in transcriptome of Littorina littorea hemocytes. Dev Comp Immunol 48(1):210–220. CrossRefPubMedGoogle Scholar
  20. 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):3320–3323CrossRefGoogle Scholar
  21. Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233(1):123–138. CrossRefPubMedGoogle Scholar
  22. 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. CrossRefPubMedGoogle Scholar
  23. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  24. Judd JW, Issitt PD (1980) The role of lectins in blood group serology. CRC Crit Rev Clin Lab Sci 12(3):171–214CrossRefGoogle Scholar
  25. 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. CrossRefGoogle Scholar
  26. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  27. 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. CrossRefPubMedGoogle Scholar
  28. Mahajan S, Ramya TNC (2018) Nature-inspired engineering of an F-type lectin for increased binding strength. Glycobiology:cwy082Google Scholar
  29. Maki M, Renkonen R (2004) Biosynthesis of 6-deoxyhexose glycans in bacteria. Glycobiology 14(3):1R–15R. CrossRefPubMedGoogle Scholar
  30. 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. CrossRefPubMedGoogle Scholar
  31. 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. CrossRefPubMedGoogle Scholar
  32. 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. CrossRefPubMedGoogle Scholar
  33. 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. CrossRefPubMedGoogle Scholar
  34. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  35. 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):30703–30708CrossRefGoogle Scholar
  36. 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. CrossRefGoogle Scholar
  37. 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. CrossRefPubMedGoogle Scholar
  38. 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):551–554CrossRefGoogle Scholar
  39. 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. CrossRefPubMedGoogle Scholar
  40. 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. CrossRefPubMedGoogle Scholar
  41. 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. CrossRefPubMedGoogle Scholar
  42. 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, LondonCrossRefGoogle Scholar
  43. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  44. Wagner M (1988) Light and electron microscopic lectin histochemistry using fluorochromes and ferritin as labels. Acta Histochem Suppl 36:115–123PubMedGoogle Scholar
  45. 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. CrossRefPubMedPubMedCentralGoogle Scholar
  46. 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. CrossRefPubMedGoogle Scholar
  47. Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  1. 1.Institute of Microbial TechnologyChandigarhIndia

Personalised recommendations