Llama peripheral B-cell populations producing conventional and heavy chain-only IgG subtypes are phenotypically indistinguishable but immunogenetically distinct

[1]  Kevin A. Henry,et al.  Immunological Functions and Evolutionary Emergence of Heavy-Chain Antibodies. , 2018, Trends in immunology.

[2]  Kevin A. Henry,et al.  Antigen recognition by single-domain antibodies: structural latitudes and constraints , 2018, mAbs.

[3]  Tomasz Magdziarz,et al.  BALCONY: an R package for MSA and functional compartments of protein variability analysis , 2018, BMC Bioinformatics.

[4]  B. Micheel,et al.  Generation of murine monoclonal antibodies with specificity against conventional camelid IgG1 and heavy-chain only IgG2/3. , 2018, Veterinary immunology and immunopathology.

[5]  J. Baardsnes,et al.  Generation of monoclonal pan-hemagglutinin antibodies for the quantification of multiple strains of influenza , 2017, PloS one.

[6]  M. van der Burg,et al.  Human IgG2- and IgG4-expressing memory B cells display enhanced molecular and phenotypic signs of maturity and accumulate with age , 2017, Immunology and cell biology.

[7]  C. Collins,et al.  Isolation of TGF-β-neutralizing single-domain antibodies of predetermined epitope specificity using next-generation DNA sequencing. , 2016, Protein engineering, design & selection : PEDS.

[8]  E. Purisima,et al.  A Rational Engineering Strategy for Designing Protein A-Binding Camelid Single-Domain Antibodies , 2016, PloS one.

[9]  Jian Wang,et al.  Comparative Analysis of Immune Repertoires between Bactrian Camel's Conventional and Heavy-Chain Antibodies , 2016, PloS one.

[10]  M. Whiteway,et al.  Deletion of a Yci1 Domain Protein of Candida albicans Allows Homothallic Mating in MTL Heterozygous Cells , 2016, mBio.

[11]  Ulrich Bodenhofer,et al.  msa: an R package for multiple sequence alignment , 2015, Bioinform..

[12]  Kevin A. Henry,et al.  Identification of cross-reactive single-domain antibodies against serum albumin using next-generation DNA sequencing. , 2015, Protein engineering, design & selection : PEDS.

[13]  Jurgen Del-Favero,et al.  Camelid Ig V genes reveal significant human homology not seen in therapeutic target genes, providing for a powerful therapeutic antibody platform , 2015, mAbs.

[14]  Michael Sattler,et al.  The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins , 2014, Proceedings of the National Academy of Sciences.

[15]  Björn Usadel,et al.  Trimmomatic: a flexible trimmer for Illumina sequence data , 2014, Bioinform..

[16]  Alastair D G Lawson,et al.  Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species. , 2014, Journal of immunological methods.

[17]  T. Baral,et al.  Single‐Domain Antibodies and Their Utility , 2013, Current protocols in immunology.

[18]  A. Cox,et al.  Investigating the candidacy of a lipoteichoic acid-based glycoconjugate as a vaccine to combat Clostridium difficile infection , 2013, Glycoconjugate Journal.

[19]  Serge Muyldermans,et al.  Nanobodies: natural single-domain antibodies. , 2013, Annual review of biochemistry.

[20]  J. Leoni,et al.  Structural analysis of effector functions related motifs, complement activation and hemagglutinating activities in Lama glama heavy chain antibodies. , 2012, Veterinary immunology and immunopathology.

[21]  Tanja Magoc,et al.  FLASH: fast length adjustment of short reads to improve genome assemblies , 2011, Bioinform..

[22]  S. Muyldermans,et al.  A Novel Promiscuous Class of Camelid Single-Domain Antibody Contributes to the Antigen-Binding Repertoire , 2010, The Journal of Immunology.

[23]  Steven J. M. Jones,et al.  Circos: an information aesthetic for comparative genomics. , 2009, Genome research.

[24]  I. Achour,et al.  Tetrameric and Homodimeric Camelid IgGs Originate from the Same IgH Locus , 2008, The Journal of Immunology.

[25]  Michael J. Osborn,et al.  Heavy chain–only antibodies are spontaneously produced in light chain–deficient mice , 2007, The Journal of experimental medicine.

[26]  C. Shoemaker,et al.  Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs). , 2007, Journal of immunological methods.

[27]  J. Appleton,et al.  Application of Monoclonal Antibodies in Functional and Comparative Investigations of Heavy-Chain Immunoglobulins in New World Camelids , 2005, Clinical Diagnostic Laboratory Immunology.

[28]  S. Muyldermans,et al.  Emergence and evolution of functional heavy-chain antibodies in Camelidae. , 2003, Developmental and comparative immunology.

[29]  S. Muyldermans,et al.  Heavy-chain antibodies in Camelidae; a case of evolutionary innovation , 2002, Immunogenetics.

[30]  Y. Durocher,et al.  High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. , 2002, Nucleic acids research.

[31]  B. de Geus,et al.  Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. , 2000, Molecular immunology.

[32]  B. de Geus,et al.  Induction of immune responses and molecular cloning of the heavy chain antibody repertoire of Lama glama. , 2000, Journal of immunological methods.

[33]  L. Wyns,et al.  Camel heavy‐chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen‐binding repertoire , 2000, The EMBO journal.

[34]  L. Frenken,et al.  The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation , 1999, Immunogenetics.

[35]  L. Wyns,et al.  LOSS OF SPLICE CONSENSUS SIGNAL IS RESPONSIBLE FOR THE REMOVAL OF THE ENTIRE CH1 DOMAIN OF THE FUNCTIONAL CAMEL IGG2A HEAVY-CHAIN ANTIBODIES' , 1999 .

[36]  Lode Wyns,et al.  Potent enzyme inhibitors derived from dromedary heavy‐chain antibodies , 1998, The EMBO journal.

[37]  S. Muyldermans,et al.  The specific variable domain of camel heavy-chain antibodies is encoded in the germline. , 1998, Journal of molecular biology.

[38]  L. Wyns,et al.  Comparison of llama VH sequences from conventional and heavy chain antibodies. , 1997, Molecular immunology.

[39]  Austin Hughes,et al.  A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks , 1995, Nature.

[40]  S. Muyldermans,et al.  Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. , 1994, Protein engineering.

[41]  S. Muyldermans,et al.  Naturally occurring antibodies devoid of light chains , 1993, Nature.

[42]  Kevin A. Henry Next-Generation DNA Sequencing of VH/VL Repertoires: A Primer and Guide to Applications in Single-Domain Antibody Discovery. , 2018, Methods in molecular biology.

[43]  V. Giudicelli,et al.  IMGT(®) tools for the nucleotide analysis of immunoglobulin (IG) and T cell receptor (TR) V-(D)-J repertoires, polymorphisms, and IG mutations: IMGT/V-QUEST and IMGT/HighV-QUEST for NGS. , 2012, Methods in molecular biology.

[44]  C. Amemiya,et al.  Distinct patterns of IgH structure and organization in a divergent lineage of chrondrichthyan fishes , 1998, Immunogenetics.