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Tsikaris, Vassilios; Petit, Marie-Christine; Orlewski, Piotr; Sakarellos‐Daitsiotis, Maria; Sakarellos, Constantinos; Τzinia, Athina K.; Konidou, Georgia; Soteriadou, Ketty; Marraud, Michel; Cung, Manh Thông

doi:10.1023/a:1008896821140

Cited by 12 publications

(18 citation statements)

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“…These findings also confirm our interpretation of the 1 H-nmr spectra concerning the behavior of the guanidinium group under various conformational states. [12][13][14][15][16] The reported study is a direct confirmation of the Arg side chain preference for participating in protonacceptor group interactions of the Yaa residue in the C-terminal sequence Arg-Xaa-Yaa. Although the nature of the Xaa and Yaa residues may affect this interaction, it is probably not possible to prevent it.…”

Section: Resultsmentioning

confidence: 63%

“…This hydrogen bonding favors the backbone folding and the structure stabilization of the model compound. [12][13][14][15][16] Conformational analysis, by 1 H-nmr spectroscopy, of the Ac-Arg-Ala-Pro-NH 2 has shown that the Arg-N H 4 protons give rise to a single and rather sharp resonance at 7.42 ppm instead of a double broad contribution expected at about 6.95 and 7.25 ppm for free protons. Also, the Arg-N H proton is downfield shifted (8.38 ppm) compared to the normal free value at 7.65 ppm.…”

Section: Introductionmentioning

confidence: 99%

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Arg side-chain-backbone interactions evidenced in model peptides by17O-NMR spectroscopy

et al. 2000

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Section: Resultsmentioning

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Arg side-chain-backbone interactions evidenced in model peptides by17O-NMR spectroscopy

et al. 2000

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“…The binding Monoclonal antibody production. The Ac-IASRYDQL specificity of mAbSRYD to the SRYD-containing peptides and octapeptide, covalently attached to the Lys-N ε H2 groups of a new to gp63 was determined by first absorbing the antibody to purisequential oligopeptide carrier (Lys-Aib-Gly) n named (SOC) n fied gp63 bound to Sepharose beads, resulting in a dramatic [28,29], was used as the immunogen [27]. The synthesis, the decrease (95%) of their binding to both the peptides and gp63.…”

Section: Methodsmentioning

confidence: 99%

Solution structures of the fibronectin‐like Leishmania gp63 SRYD‐containing sequence in the free and antibody‐bound states

Petit¹,

Orlewski²,

Tsikaris³

et al. 1998

European Journal of Biochemistry

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The anti-SRYD monoclonal antibody (mAbSRYD) raised against the IASRYDQL synthetic octapeptide, the 250Ϫ257 sequence of the Leishmania major surface glycoprotein gp63 recognizes both SRYDcontaining peptides and the whole cognate major surface protein on intact parasites. Two SRYD-containing peptides, which antigenically and functionally mimic the RGDS sequence of fibronectin and efficiently inhibit parasite attachment to the macrophage receptors, were studied by two-dimensional transferred nuclear Overhauser effect experiments in the presence of mAbSRYD. The antibody-bound IASRYDQL octapeptide solution conformation was determined on the basis of 55 interproton-distance restraints, derived from NMR measurements. Eighteen structures which were first generated using an approach combining distance geometry and molecular dynamics, converge by energy minimization toward a folded structure with an average rmsd from the experimental data of less than 0.05 nm for the overall backbone and 0.025 nm for the SRYD motif. A distorted γ-turn was found, stabilized by the backboneϪ backbone D255-NH to R253-CO hydrogen bond, while the R253 and D255 side chains are pointing in opposite directions. This latter antibody-bound structure is compared with that of the free octapeptide in dimethylsulfoxide solution, and with the crystal structure of the RYD fragment in OPG2 Fab, an antireceptor antibody that mimics the RGD cell adhesion site. On this basis, a mechanism for IASRYDQLϪ receptor interaction is discussed.Keywords : antigen-antibody interaction ; Leishmania gp63; molecular dynamics; SRYD motif; transferred NOE.Leishmania are obligate intracellular protozoan parasites promoting receptors, the integrins [15]. The functional importance of gp63 in the binding of promastigotes to macrophages which cause a group of diseases in humans, ranging from selfhas been also demonstrated using genetic approaches [16,17]. healing cutaneous lesions to severe visceral leishmaniasis or Antibodies against fibronectin and RGDS-containing fibroKala-Azar with a high fatality rate. The attachment of Leishnectin peptides bind to a single specific region of gp63, i.e. mania promastigotes to macrophages, crucial for intracellular SRYD, localized between residues 252 and 255 [18]. Also, satuparasitism at the early phase of infection, has been demonstrated ration of macrophage receptors by synthetic SRYD-containing to be a specific receptor-mediated event. Considerable interest peptides resulted in approximately 70% inhibition of promastihas been focused on the gp63 surface glycoprotein [1Ϫ7], the gote attachment to macrophages [18]. It was concluded that the major antigenic protein of most Leishmania promastigotes [8], SRYD moiety represents the putative adhesion site of gp63 with not only due to its potential use as a vaccine component [9Ϫ14] macrophages and mimics the RGDS-fibronectin properties for but also due to its role in cell adhesion. It has been suggested cell attachment. Mutations at the SRYD adhesion site of gp63 that gp63, a necessary ligand ...

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“…14,15 Polytuftsin built up from repeat unit of the naturally occurring tetrapeptide tuftsin (TKPR). 16 Tuftsin is a fragment (289 -292) of the IgG Fc heavy chain that is known to modulate the antigen-presenting capacity of macrophages.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, conformation, and immunoreactivity of new carrier molecules based on repeated tuftsin‐like sequence

et al. 2004

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Sequential oligopeptides based on a pentapeptide (TKPKG) derived from tuftsin with different lengths were synthesized by stepwise solid phase methodology. These highly soluble oligomers were nontoxic on mouse spleen cells, and other biological data suggested that tuftsin-like properties were also presented. The (TKPKG)n (n=2,4,6,8) oligopeptides were not immunogenic; however, they increased sheep red blood cells (SRBC) antigen specific antibody response in mice, demonstrating their immunostimulatory effect. Chemotactic activity was also found on J774 monocyte cells, while MRC5 fibroblasts were chemotactically nonresponders to the tested forms of tuftsin. These oligomers showed unordered and flexible structure by CD measurements, confirmed by computer modeling studies indicating also a fairly good accessibility of the epsilon-amino group of each lysine residue. Data suggest that these new oligotuftsin derivatives can be considered as promising carriers for synthetic vaccine.

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Cited by 12 publications

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Arg side-chain-backbone interactions evidenced in model peptides by17O-NMR spectroscopy

Arg side-chain-backbone interactions evidenced in model peptides by17O-NMR spectroscopy

Solution structures of the fibronectin‐like Leishmania gp63 SRYD‐containing sequence in the free and antibody‐bound states

Synthesis, conformation, and immunoreactivity of new carrier molecules based on repeated tuftsin‐like sequence

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