Globular-shaped variable lymphocyte receptors B antibody multimerized by a hydrophobic clustering in hagfish

In hagfish and lampreys, two representative jawless vertebrates, the humoral immunity is directly mediated by variable lymphocyte receptors B (VLRBs). Both monomeric VLRBs are structurally and functionally similar, but their C-terminal tails differ: lamprey VLRB has a Cys-rich tail that forms disulf...

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Bibliographic Details
Published in:Scientific reports 2018-07, Vol.8 (1), p.10801-10, Article 10801
Main Authors: Kim, Jaesung, Im, Se Pyeong, Lee, Jung Seok, Lazarte, Jassy Mary S., Kim, Si Won, Jung, Jae Wook, Kim, Jong Yong, Kim, Young Rim, Lee, Sangmin, Kim, Gwang Joong, Jung, Hyun Suk, Lee, Kyun Oh, Adams, Alexandra, Thompson, Kim D., Jung, Tae Sung
Format: Article
Language:English
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C-Terminus
Electron microscopy
Humanities and Social Sciences
Humoral immunity
Hydrophobicity
Immune system
Localization
Lymphocyte receptors
Lymphocytes
Lymphocytes B
multidisciplinary
Science
Science (multidisciplinary)
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Summary:In hagfish and lampreys, two representative jawless vertebrates, the humoral immunity is directly mediated by variable lymphocyte receptors B (VLRBs). Both monomeric VLRBs are structurally and functionally similar, but their C-terminal tails differ: lamprey VLRB has a Cys-rich tail that forms disulfide-linked pentamers of dimers, contributing to its multivalency, whereas hagfish VLRB has a superhydrophobic tail of unknown structure. Here, we reveal that VLRBs obtained from hagfish plasma have a globular-shaped multimerized form (approximately 0.6 to 1.7 MDa) that is generated by hydrophobic clustering instead of covalent linkage. Electron microscopy (EM) and single-particle analysis showed that the multimerized VLRBs form globular-shaped clusters with an average diameter of 28.7 ± 2.2 nm. The presence of VLRBs in the complex was confirmed by immune-EM analysis using an anti-VLRB antibody. Furthermore, the hydrophobic hagfish C-terminus (HC) was capable of triggering multimerization and directing the cellular surface localization via a glycophosphatidylinositol linkage. Our results strongly suggest that the hagfish VLRB forms a previously unknown globular-shaped antibody. This novel identification of a structurally unusual VLRB complex may suggest that the adaptive immune system of hagfish differs from that of lamprey.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-018-29197-w