Evolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regions.

Schluter, Samuel F.; Hohman, Valerie S.; Edmundson, Allen B.; Marchalonis, John J.

doi:10.1073/pnas.86.24.9961

Cited by 33 publications

(16 citation statements)

References 25 publications

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“…As well as the comparisons of human and shark VH domains presented here, it has been readily feasible to correlate the sequences and structures of sandbar shark VÏ and CÏ domains using characterized human Ï-chains such as Mcg as a template [for a discussion, see ref. 59].…”

Section: Functional Similarities Between the Antibodies Of Sharks Andmentioning

confidence: 99%

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

Ramsland

Kaushik

Marchalonis

et al. 2001

Exp Clin Immunogenet

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Available data suggest that ‘primitive’ antibody-combining sites often include longer than average HCDR3s. Long HCDR3 sequences have been reported in diverse vertebrates, including humans, cattle, camels and sharks. These long HCDR3 segments contain unusual sequence features such as stretches of Gly or Pro residues and multiple Cys residues. We examined how longer than average HCDR3s were accommodated in the V domains of human, murine and camel antibodies with known three-dimensional structures. The main conclusions were that (1) HCDR3s longer than 12 residues should protrude outward from the V domains; (2) descending HCDR3 polypeptides may utilize VL (including LCDR3) constituents as a platform, supporting the protruding segments; (3) intra- and inter-HCDR disulfides are frequently formed to rigidify the structure of HCDR3 or the combining site, and (4) V and C domains were possibly more similar in primordial antibodies than they are in their present day counterparts.

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Section: Functional Similarities Between the Antibodies Of Sharks Andmentioning

confidence: 99%

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

Ramsland

Kaushik

Marchalonis

et al. 2001

Exp Clin Immunogenet

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“…Furthermore, additional L chain classes may exist in elasmobranchs which are neither K-like nor A-like. We conclude that L chain class diversity is more extensive in representatives of primitive vertebrate classes than previously realized (7).…”

Section: Discussionmentioning

confidence: 39%

“…4 and 28); sequences not given in ref. 37 are sandbar shark A (7,8), homed shark A (9), Xenopus L2 Vl and L2 (5), and R. catesbeiana (6). The branch order was modified to optimize the least-squares fit of distances along branches to the distance scores of pairs of aligned sequences.…”

Section: Sedrk-svl-----seei/ds-w---s--vs--k-gfr-l-rv-dketds--t-gtvstdmentioning

confidence: 99%

“…The finding of only A-like L chains in sharks led to the hypothesis that only one L chain isotype would be found in representatives of primitive vertebrate classes (7). Furthermore, the presence of A-like L chains in a chondricthyian led to the suggestion that A may have been the first isotype to emerge in evolution (9).…”

mentioning

confidence: 99%

“…The L chain constant (C) domain of another amphibian, Rana catesbeiana, cannot be clearly classified as CK or CA (6). A-like L chains are present in two species of sharks (7)(8)(9).…”

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confidence: 99%

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Isolation of a shark immunoglobulin light chain cDNA clone encoding a protein resembling mammalian kappa light chains: implications for the evolution of light chains.

Greenberg

Steiner

Kasahara

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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The time of emergence of immunoglobulin K and A light (L) chains in evolution is unknown. An L chain cDNA clone was isolated from the nurse shark (Ginglymostoma cirratum), a cartilaginous fish, whose predicted variable (V) region amino acid sequence has up to 60% sequence identity to mammalian V, domains. Genomic analyses suggest a clustertpe gene organization for this L chain locus, similar to the shark A-like immunoglobulin L chain loci rather than mammalian K loci. We propose that divergence of the ancestral L chain into isotypes likely occurred before the emergence of elasmobranchs 400-450 million years ago. Similarities in gene organization between the two isotypes in sharks may reflect the gene organization utilized by the ancestral L chain.Immunoglobulins are the central effector proteins in the humoral adaptive immune system and are composed of two heavy (H) and two light (L) (8,17).The finding of only A-like L chains in sharks led to the hypothesis that only one L chain isotype would be found in representatives of primitive vertebrate classes (7). Furthermore, the presence of A-like L chains in a chondricthyian led to the suggestion that A may have been the first isotype to emerge in evolution (9). However, the presence of other isotypes in sharks was not ruled out (9, 18), and phylogeneticThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.trees of all described K and A suggested that the ancestor of sharks and all other vertebrates possessed both isotypes (4). We report here the isolation of an L chain cDNA clone from the nurse shark, Ginglymostoma cirratum. ¶ The predicted V region amino acid sequence is similar to mammalian VK (60% identity). This L chain differs from all other K described in that it has a cluster-type gene organization similar to the shark H (19) and A-like loci (8, 17). MATERIALS AND METHODSOligonucleotides and PCR. The following three oligonucleotides were used for amplification of nurse shark cDNA: the immunoglobulin-superfamily-specific CB2 primer (described in Results; 5'-GCGAATTCAARGCNACNCTBGTNTG-3', where N represents A, C, G, or T, R is A or G, and B is G, T, or C), an adapter primer (5'-GACTCGAGTCGACATCG-3') (20), and a (dT)17 adapter primer (5'-GACTCGAGTCGA-CATCGATTTTTTTTTTTTTTTTT-3') (20). The first eight bases of CB2 contain an EcoRI recognition sequence. Preparation of poly(A)+ RNA and its reverse transcription with the (dT)17 adapter primer were done as previously described (21). The PCR mixture (50 ,ul) contained 3 Al of cDNA, 200 ,uM dNTPs, 0.5 ,uM CB2 primer, 0.5 ,uM adapter primer, S ul of lOx reaction buffer (Stratagene), and 2.5 units of Taq DNA polymerase (Stratagene). The amplification protocol used was three cycles of 1 min at 94°C, 2 min at 37°C, and 3 min at 72°C with a ramp time of 4 sec/°C as suggested in ref. 22; followed by 30 cycles of 1 min at 94°C, 2 min at 55°C, and 3 min at 72°C with...

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Binding of Peptides to Proteins: An Exercise in Molecular Design

Tribbick³

et al. 2007

Ciba Foundation Symposium 158 ‐ Host‐Guest Molecular Interactions: From Chemistry to Biology

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Evolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regions.

Cited by 33 publications

References 25 publications

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

Isolation of a shark immunoglobulin light chain cDNA clone encoding a protein resembling mammalian kappa light chains: implications for the evolution of light chains.

Binding of Peptides to Proteins: An Exercise in Molecular Design

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