Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype
Abstract
A physical and mathematical model identifies similarities between phosphocholine-binding antibodies.A methodology based on the representation of each amino acid of a protein sequence by the electron-ion interaction potential and subsequent analysis by signal processing was used to determine the characteristic or common frequency (in Hz) that reflects the biological activity shared among phosphocholine (PC)-binding antibodies. The common frequency for the variable portion of the heavy chain (VH) of the PC-specific antibodies is found to be at f 0.37 Hz. The VH sequences of the PC-binding antibodies exhibit three subsites for the PC moiety where hypervariable region 2 (CDR2) plays a role in the interaction with the phosphate group. Mutations in this VH region have an impact on the ability of mutant variants to bind PC and its carrier molecule, as well as on the characteristic frequency shift toward f 0.12 Hz for mutants failing to bind both hapten and carrier. The VH sequence of mutants ...that retain the ability to bind PC still shows f 0.37 Hz, suggesting that this frequency determines PC binding. However, this statement was not confirmed as mutation in another PC subsite impairs PC binding but retains both the phosphate-group recognition and the frequency at f 0.37 Hz. Herein, this finding is discussed to promote the idea that the VH sequence of the PC-binding antibodies encodes the subsite for phosphate-group binding as a dominant functional activity and that only CDR2 of the T15-idiotype antibodies together with FR3 region form an autonomous self-association function represented by the T15VH5073 peptide with f 0.370.05 Hz. Thus, these data confirmed that T15VH50-73 peptide might be used in superantibody technology.
Keywords:
antibodies with autophilic properties / informational spectrum method / resonant recognition model / superantibodiesSource:
International Immunology, 2013, 25, 6, 345-352Funding / projects:
- A new approach to foundational problems of quantum mechanics related to applications in quantum technologies and interpretations of signals of various origins (RS-MESTD-Basic Research (BR or ON)-171028)
- Pharmacodynamic and pharmacogenomic research of new drugs in the treatment of solid tumors (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-41026)
DOI: 10.1093/intimm/dxs156
ISSN: 0953-8178
PubMed: 23382353
WoS: 000319467000002
Scopus: 2-s2.0-84878452059
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VinčaTY - JOUR AU - Srdić-Rajić, Tatjana AU - Keković, Goran AU - Davidović, Dragomir M. AU - Metlaš, Radmila PY - 2013 UR - https://vinar.vin.bg.ac.rs/handle/123456789/5519 AB - A physical and mathematical model identifies similarities between phosphocholine-binding antibodies.A methodology based on the representation of each amino acid of a protein sequence by the electron-ion interaction potential and subsequent analysis by signal processing was used to determine the characteristic or common frequency (in Hz) that reflects the biological activity shared among phosphocholine (PC)-binding antibodies. The common frequency for the variable portion of the heavy chain (VH) of the PC-specific antibodies is found to be at f 0.37 Hz. The VH sequences of the PC-binding antibodies exhibit three subsites for the PC moiety where hypervariable region 2 (CDR2) plays a role in the interaction with the phosphate group. Mutations in this VH region have an impact on the ability of mutant variants to bind PC and its carrier molecule, as well as on the characteristic frequency shift toward f 0.12 Hz for mutants failing to bind both hapten and carrier. The VH sequence of mutants that retain the ability to bind PC still shows f 0.37 Hz, suggesting that this frequency determines PC binding. However, this statement was not confirmed as mutation in another PC subsite impairs PC binding but retains both the phosphate-group recognition and the frequency at f 0.37 Hz. Herein, this finding is discussed to promote the idea that the VH sequence of the PC-binding antibodies encodes the subsite for phosphate-group binding as a dominant functional activity and that only CDR2 of the T15-idiotype antibodies together with FR3 region form an autonomous self-association function represented by the T15VH5073 peptide with f 0.370.05 Hz. Thus, these data confirmed that T15VH50-73 peptide might be used in superantibody technology. T2 - International Immunology T1 - Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype VL - 25 IS - 6 SP - 345 EP - 352 DO - 10.1093/intimm/dxs156 ER -
@article{ author = "Srdić-Rajić, Tatjana and Keković, Goran and Davidović, Dragomir M. and Metlaš, Radmila", year = "2013", abstract = "A physical and mathematical model identifies similarities between phosphocholine-binding antibodies.A methodology based on the representation of each amino acid of a protein sequence by the electron-ion interaction potential and subsequent analysis by signal processing was used to determine the characteristic or common frequency (in Hz) that reflects the biological activity shared among phosphocholine (PC)-binding antibodies. The common frequency for the variable portion of the heavy chain (VH) of the PC-specific antibodies is found to be at f 0.37 Hz. The VH sequences of the PC-binding antibodies exhibit three subsites for the PC moiety where hypervariable region 2 (CDR2) plays a role in the interaction with the phosphate group. Mutations in this VH region have an impact on the ability of mutant variants to bind PC and its carrier molecule, as well as on the characteristic frequency shift toward f 0.12 Hz for mutants failing to bind both hapten and carrier. The VH sequence of mutants that retain the ability to bind PC still shows f 0.37 Hz, suggesting that this frequency determines PC binding. However, this statement was not confirmed as mutation in another PC subsite impairs PC binding but retains both the phosphate-group recognition and the frequency at f 0.37 Hz. Herein, this finding is discussed to promote the idea that the VH sequence of the PC-binding antibodies encodes the subsite for phosphate-group binding as a dominant functional activity and that only CDR2 of the T15-idiotype antibodies together with FR3 region form an autonomous self-association function represented by the T15VH5073 peptide with f 0.370.05 Hz. Thus, these data confirmed that T15VH50-73 peptide might be used in superantibody technology.", journal = "International Immunology", title = "Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype", volume = "25", number = "6", pages = "345-352", doi = "10.1093/intimm/dxs156" }
Srdić-Rajić, T., Keković, G., Davidović, D. M.,& Metlaš, R.. (2013). Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype. in International Immunology, 25(6), 345-352. https://doi.org/10.1093/intimm/dxs156
Srdić-Rajić T, Keković G, Davidović DM, Metlaš R. Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype. in International Immunology. 2013;25(6):345-352. doi:10.1093/intimm/dxs156 .
Srdić-Rajić, Tatjana, Keković, Goran, Davidović, Dragomir M., Metlaš, Radmila, "Phosphocholine-binding antibody activities are hierarchically encoded in the sequence of the heavy-chain variable region: dominance of self-association activity in the T15 idiotype" in International Immunology, 25, no. 6 (2013):345-352, https://doi.org/10.1093/intimm/dxs156 . .