Nature Structural and Molecular Biology, volume 16, issue 7, pages 725-730

Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen

C.Alejandro Velikovsky ¹

Lu Deng ¹

Satoshi Tasumi ²

Lakshminarayan M Iyer ³

Melissa C Kerzic ¹

L Aravind ³

ZEEV PANCER ²

Roy A. Mariuzza ¹

Hide authors affiliations Show authors affiliations: 3 affiliations

Center for Advanced Research in Biotechnology, WM Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, Rockville, USA |

Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, USA |

National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, USA |

Publication type: Journal Article

Publication date: 2009-06-21

Springer Nature

Journal: Nature Structural and Molecular Biology

Quartile SCImago

Quartile WOS

Impact factor: 16.8

ISSN: 15459993, 15459985

DOI: 10.1038/nsmb.1619

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Molecular Biology

Structural Biology

Abstract

The lamprey adaptive immune system is evolutionarily distinct from ours and based on recognition by leucine-rich repeat proteins rather than antibodies. The crystal structure of a lamprey variable lymphocyte receptor in complex with a protein antigen now gives insight into how a distinct adaptive immune molecule recognizes a protein antigen. Variable lymphocyte receptors (VLRs) are leucine-rich repeat proteins that mediate adaptive immunity in jawless vertebrates. VLRs are fundamentally different from the antibodies of jawed vertebrates, which consist of immunoglobulin (Ig) domains. We determined the structure of an anti–hen egg white lysozyme (HEL) VLR, isolated by yeast display, bound to HEL. The VLR, whose affinity resembles that of IgM antibodies, uses nearly all its concave surface to bind the protein, in addition to a loop that penetrates into the enzyme active site. The VLR–HEL structure combined with sequence analysis revealed an almost perfect match between ligand-contacting positions and positions with highest sequence diversity. Thus, it is likely that we have defined the generalized antigen-binding site of VLRs. We further demonstrated that VLRs can be affinity-matured by 13-fold to affinities as high as those of IgG antibodies, making VLRs potential alternatives to antibodies for biotechnology applications.

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Citations by journals

	1 2 3 4 5 6 7 8
Proceedings of the National Academy of Sciences of the United States of America	Proceedings of the National Academy of Sciences of the United States of America, 8, 8.33% Proceedings of the National Academy of Sciences of the United States of America 8 publications, 8.33%
Journal of Biological Chemistry	Journal of Biological Chemistry, 4, 4.17% Journal of Biological Chemistry 4 publications, 4.17%
Fish and Shellfish Immunology	Fish and Shellfish Immunology, 4, 4.17% Fish and Shellfish Immunology 4 publications, 4.17%
Journal of Immunology	Journal of Immunology, 3, 3.13% Journal of Immunology 3 publications, 3.13%
PLoS ONE	PLoS ONE, 3, 3.13% PLoS ONE 3 publications, 3.13%
Structure	Structure, 3, 3.13% Structure 3 publications, 3.13%
Molecular Immunology	Molecular Immunology, 3, 3.13% Molecular Immunology 3 publications, 3.13%
Cells	Cells, 2, 2.08% Cells 2 publications, 2.08%
Frontiers in Immunology	Frontiers in Immunology, 2, 2.08% Frontiers in Immunology 2 publications, 2.08%
Biochimica et Biophysica Acta - Proteins and Proteomics	Biochimica et Biophysica Acta - Proteins and Proteomics, 2, 2.08% Biochimica et Biophysica Acta - Proteins and Proteomics 2 publications, 2.08%
Journal of Immunological Methods	Journal of Immunological Methods, 2, 2.08% Journal of Immunological Methods 2 publications, 2.08%
European Journal of Immunology	European Journal of Immunology, 2, 2.08% European Journal of Immunology 2 publications, 2.08%
Advances in Experimental Medicine and Biology	Advances in Experimental Medicine and Biology, 2, 2.08% Advances in Experimental Medicine and Biology 2 publications, 2.08%
Advances in Immunology	Advances in Immunology, 2, 2.08% Advances in Immunology 2 publications, 2.08%
Annual Review of Immunology	Annual Review of Immunology, 2, 2.08% Annual Review of Immunology 2 publications, 2.08%
JCI insight	JCI insight, 1, 1.04% JCI insight 1 publication, 1.04%
Immunotherapy	Immunotherapy, 1, 1.04% Immunotherapy 1 publication, 1.04%
Acta Crystallographica Section F Structural Biology and Crystallization Communications	Acta Crystallographica Section F Structural Biology and Crystallization Communications, 1, 1.04% Acta Crystallographica Section F Structural Biology and Crystallization Communications 1 publication, 1.04%
Cancer journal (Sudbury, Mass.)	Cancer journal (Sudbury, Mass.), 1, 1.04% Cancer journal (Sudbury, Mass.) 1 publication, 1.04%
Communications Biology	Communications Biology, 1, 1.04% Communications Biology 1 publication, 1.04%
Biology Direct	Biology Direct, 1, 1.04% Biology Direct 1 publication, 1.04%
Scientific Reports	Scientific Reports, 1, 1.04% Scientific Reports 1 publication, 1.04%
Plant Methods	Plant Methods, 1, 1.04% Plant Methods 1 publication, 1.04%
Nature Reviews Genetics	Nature Reviews Genetics, 1, 1.04% Nature Reviews Genetics 1 publication, 1.04%
Nature Reviews Immunology	Nature Reviews Immunology, 1, 1.04% Nature Reviews Immunology 1 publication, 1.04%
Immunogenetics	Immunogenetics, 1, 1.04% Immunogenetics 1 publication, 1.04%
Fish Physiology and Biochemistry	Fish Physiology and Biochemistry, 1, 1.04% Fish Physiology and Biochemistry 1 publication, 1.04%
Current Opinion in Plant Biology	Current Opinion in Plant Biology, 1, 1.04% Current Opinion in Plant Biology 1 publication, 1.04%
Current Opinion in Immunology	Current Opinion in Immunology, 1, 1.04% Current Opinion in Immunology 1 publication, 1.04%
	1 2 3 4 5 6 7 8

Citations by publishers

	5 10 15 20 25 30 35
Elsevier	Elsevier, 33, 34.38% Elsevier 33 publications, 34.38%
Springer Nature	Springer Nature, 11, 11.46% Springer Nature 11 publications, 11.46%
Wiley	Wiley, 9, 9.38% Wiley 9 publications, 9.38%
Proceedings of the National Academy of Sciences (PNAS)	Proceedings of the National Academy of Sciences (PNAS), 8, 8.33% Proceedings of the National Academy of Sciences (PNAS) 8 publications, 8.33%
American Society for Biochemistry and Molecular Biology	American Society for Biochemistry and Molecular Biology, 4, 4.17% American Society for Biochemistry and Molecular Biology 4 publications, 4.17%
Annual Reviews	Annual Reviews, 4, 4.17% Annual Reviews 4 publications, 4.17%
The American Association of Immunologists	The American Association of Immunologists, 3, 3.13% The American Association of Immunologists 3 publications, 3.13%
Public Library of Science (PLoS)	Public Library of Science (PLoS), 3, 3.13% Public Library of Science (PLoS) 3 publications, 3.13%
Multidisciplinary Digital Publishing Institute (MDPI)	Multidisciplinary Digital Publishing Institute (MDPI), 2, 2.08% Multidisciplinary Digital Publishing Institute (MDPI) 2 publications, 2.08%
Frontiers Media S.A.	Frontiers Media S.A., 2, 2.08% Frontiers Media S.A. 2 publications, 2.08%
Oxford University Press	Oxford University Press, 2, 2.08% Oxford University Press 2 publications, 2.08%
American Society for Clinical Investigation	American Society for Clinical Investigation, 1, 1.04% American Society for Clinical Investigation 1 publication, 1.04%
Future Medicine	Future Medicine, 1, 1.04% Future Medicine 1 publication, 1.04%
International Union of Crystallography (IUCr)	International Union of Crystallography (IUCr), 1, 1.04% International Union of Crystallography (IUCr) 1 publication, 1.04%
Wolters Kluwer Health	Wolters Kluwer Health, 1, 1.04% Wolters Kluwer Health 1 publication, 1.04%
American Chemical Society (ACS)	American Chemical Society (ACS), 1, 1.04% American Chemical Society (ACS) 1 publication, 1.04%
EMBO press	EMBO press, 1, 1.04% EMBO press 1 publication, 1.04%
Walter de Gruyter	Walter de Gruyter, 1, 1.04% Walter de Gruyter 1 publication, 1.04%
American Association for the Advancement of Science (AAAS)	American Association for the Advancement of Science (AAAS), 1, 1.04% American Association for the Advancement of Science (AAAS) 1 publication, 1.04%
American Association for Cancer Research (AACR)	American Association for Cancer Research (AACR), 1, 1.04% American Association for Cancer Research (AACR) 1 publication, 1.04%
eLife Sciences Publications	eLife Sciences Publications, 1, 1.04% eLife Sciences Publications 1 publication, 1.04%
Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii	Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii, 1, 1.04% Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii 1 publication, 1.04%
	5 10 15 20 25 30 35

We do not take into account publications without a DOI.
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GOST |

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GOST Copy

Velikovsky C. et al. Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen // Nature Structural and Molecular Biology. 2009. Vol. 16. No. 7. pp. 725-730.

GOST all authors (up to 50) Copy

Velikovsky C., Deng L., Tasumi S., Iyer L. M., Kerzic M. C., Aravind L., PANCER Z., Mariuzza R. A. Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen // Nature Structural and Molecular Biology. 2009. Vol. 16. No. 7. pp. 725-730.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1038/nsmb.1619

UR - https://doi.org/10.1038/nsmb.1619

TI - Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen

T2 - Nature Structural and Molecular Biology

AU - Velikovsky, C.Alejandro

AU - Deng, Lu

AU - Tasumi, Satoshi

AU - Iyer, Lakshminarayan M

AU - Kerzic, Melissa C

AU - Aravind, L

AU - PANCER, ZEEV

AU - Mariuzza, Roy A.

PY - 2009

DA - 2009/06/21 00:00:00

PB - Springer Nature

SP - 725-730

IS - 7

VL - 16

SN - 1545-9993

SN - 1545-9985

ER -

BibTex |

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BibTex Copy

@article{2009_Velikovsky,

author = {C.Alejandro Velikovsky and Lu Deng and Satoshi Tasumi and Lakshminarayan M Iyer and Melissa C Kerzic and L Aravind and ZEEV PANCER and Roy A. Mariuzza},

title = {Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen},

journal = {Nature Structural and Molecular Biology},

year = {2009},

volume = {16},

publisher = {Springer Nature},

month = {jun},

url = {https://doi.org/10.1038/nsmb.1619},

number = {7},

pages = {725--730},

doi = {10.1038/nsmb.1619}

}

MLA

Cite this

MLA Copy

Velikovsky, C.Alejandro, et al. “Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen.” Nature Structural and Molecular Biology, vol. 16, no. 7, Jun. 2009, pp. 725-730. https://doi.org/10.1038/nsmb.1619.

Found error?

Publisher

Springer Nature

Journal

Nature Structural and Molecular Biology

Quartile SCImago

Quartile WOS

Impact factor

16.8

ISSN

15459993 (Print)
15459985 (Electronic)