Structure of a third murine immunoglobulin lambda light chain variable region that is expressed in laboratory mice.

Sanchez, Pierre; Marche, Patrice N.; Guern, Christian Le; Cazenave, Pierre‐André

doi:10.1073/pnas.84.24.9185

Cited by 36 publications

(10 citation statements)

References 37 publications

(23 reference statements)

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“…Furthermore, there is a sequence homology of 75% found between complementarity determining region (CDR) 3 of F28C4 VL and VH and the V-D-J junction of the TCR V ␤ 8.2 from encephalitogenic T cells. This homology is not shared by other Ig CDR3 regions and arises, in part, because F28C4 uses an unusual L chain V region known as V x (14,15). Before the demonstration that an Ab with V x could bind MBP, no Ab with such an L chain had any known specificity.…”

Section: Experimental Allergic Encephalomyelitis (Eae)mentioning

confidence: 99%

“…V x-containing Ig from normal BALB/c mouse sera (Sigma Chemical Co., St. Louis, MO) was purified over a anti-V x Ab Sepharose 4B affinity column prepared using the monospecific rabbit anti-V x Ab described above. V x-containing Abs represented ‫ف‬ 0.5% of total Ig as previously described (15).…”

Section: Methodsmentioning

confidence: 99%

“…Before the demonstration that an Ab with V x could bind MBP, no Ab with such an L chain had any known specificity. V x is an unusual V gene segment that was discovered in 1987 in polyclonally activated B cells (14,15). V x rearranges with J 2-C 2 and displays at least three unique features: First, its amino acid sequence is only 30-33% homologous to any other known V and/or V-kappa ( ) genes.…”

Section: Experimental Allergic Encephalomyelitis (Eae)mentioning

confidence: 99%

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Murine V lambda x and V lambda x-containing antibodies bind human myelin basic protein.

Galin¹,

Maier²,

Zhou³

et al. 1996

J. Clin. Invest.

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Myelin basic protein (MBP) is highly immunogenic and a known autoantigen capable of inducing experimental allergic encephalomyelitis (EAE), the animal model of multiple sclerosis. We have previously described a murine monoclonal antibody (mAb), F28C4, directed against the encephalitogenic MBP peptide acetyl (Ac) 1-9, which contains a V x light chain. Considering the rarity of V x usage, we determined whether other Abs having V x light chains shared similar antigen (Ag) specificity. We screened a panel of

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Section: Experimental Allergic Encephalomyelitis (Eae)mentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Experimental Allergic Encephalomyelitis (Eae)mentioning

confidence: 99%

See 1 more Smart Citation

Murine V lambda x and V lambda x-containing antibodies bind human myelin basic protein.

Galin¹,

Maier²,

Zhou³

et al. 1996

J. Clin. Invest.

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“…Interestingly, 13F6-1-2 contains a rare Vλ x light chain which is observed in only 0.5% of antibody sequences and is barely detectable in normal mouse serum [17][18][19] . Vλ x , first described in 1987 [17][18][19] , is conserved among mice, humans, and other mammals 20 , and displays at least three features unique from Vλ1 and Vλ2.…”

Section: Introductionmentioning

confidence: 99%

“…Vλ x , first described in 1987 [17][18][19] , is conserved among mice, humans, and other mammals 20 , and displays at least three features unique from Vλ1 and Vλ2. The amino acid sequence is only ~30-33% homologous to other known Vλ and/or Vκ light chains.…”

Section: Introductionmentioning

confidence: 99%

Complex of a Protective Antibody with Its Ebola Virus GP Peptide Epitope: Unusual Features of a Vλx Light Chain

Lee

Kuehne

Abelson

et al. 2008

Journal of Molecular Biology

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Abstract13F6-1-2 is a murine monoclonal antibody that recognizes the heavily glycosylated mucin-like domain of the Ebola virus virion-attached glycoprotein (GP) and protects animals against lethal viral challenge. Here we present the crystal structure, at 2.0 Å, of 13F6-1-2 in complex with its Ebola virus GP peptide epitope. The GP peptide binds in an extended conformation, anchored primarily by interactions to the heavy chain. Two GP residues, Gln P406 and Arg P409, make extensive side chain hydrogen bond and electrostatic interactions to the antibody and are likely critical for recognition and affinity. The 13F6-1-2 antibody utilizes a rare Vλ x light chain. The three light chain complementarity determining regions (CDRs) do not adopt canonical conformations and represent new classes of structures distinct from Vκ and other Vλ light chains. In addition, although Vλ x had been thought to confer specificity, all light chain contacts are mediated through germline-encoded residues. This structure of an antibody that protects against the Ebola virus now provides a framework for humanization and development of a post-exposure immunotherapeutic.

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Proteome analysis of activated murine B-lymphocytes

Frey¹,

Fountoulakis

Lefkovits³

2000

Electrophoresis

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Proteins extracted from murine B-lymphocytes after in vitro stimulation by lipopolysaccharide were separated by two-dimensional (2-D) polyacrylamide gel electrophoresis and analyzed by matrix assisted laser desorption/ionization mass spectrometry. Structural information on the protein entities from 153 spots was obtained. Since many of these spots occur as members of spot families, a smaller number --98 genes-- was found to be coding for the identified spots. The elucidated proteins belong to groups of functional categories; we found 26 enzymes, 36 regulatory proteins, 15 chaperones, 15 structural proteins, 4 immunoglobulins, 1 ribosomal and 1 histone protein. A comparison between expected and observed molecular masses yields a good correlation for the majority of the compared spot entities. This set of proteins now identified in the context of a lymphocyte 2-D gel pattern should advance further studies on lymphocyte functions.

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Structure of a third murine immunoglobulin lambda light chain variable region that is expressed in laboratory mice.

Abstract: Recently, we reported evidence for the existence of an immunoglobulin X light chain (Ax) whose variable region differs from those encoded by the known Vk gene

Cited by 36 publications

References 37 publications

Murine V lambda x and V lambda x-containing antibodies bind human myelin basic protein.

Murine V lambda x and V lambda x-containing antibodies bind human myelin basic protein.

Complex of a Protective Antibody with Its Ebola Virus GP Peptide Epitope: Unusual Features of a Vλx Light Chain

Proteome analysis of activated murine B-lymphocytes

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