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Chaperone Skp from Yersinia pseudotuberculosis exhibits immunoglobulin G binding ability

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Abstract

A low-molecular-weight cationic protein that can bind human and rabbit immunoglobulins G has been isolated from Yersinia pseudotuberculosis cells. This immunoglobulin binding protein (IBP) interacts with IgG Fc-fragment, the association constant of the resulting complex being 3.1 μM−1. MALDI-TOF mass spectrometry analysis of IBP revealed its molecular mass of 16.1 kDa, and capillary isoelectrofocusing analysis showed pI value of 9.2. N-Terminal sequence determination by Edman degradation revealed the sequence of the 15 terminal amino acid residues (ADKIAIVNVSSIFQ). Tryptic hydrolysate of IBP was subjected to MALDI-TOF mass spectrometry for proteolytic peptide profiling. Based on the peptide fingerprint, molecular mass, pI, and N-terminal sequence and using bioinformatic resources, IBP was identified as Y. pseudotuberculosis periplasmic chaperone Skp. Using the method of comparative modeling a spatial model of Skp has been built. This model was then used for modeling of Skp complexes with human IgG1 Fc-fragment by means of molecular docking.

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Abbreviations

IBP:

immunoglobulin binding protein

Skp:

seventeen kilodalton protein

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Authors and Affiliations

  1. Pacific Institute of Bioorganic Chemistry, Far East Division of the Russian Academy of Sciences, pr. 100-letiya Vladivostoka 159, 690022, Vladivostok, Russia

    E. V. Sidorin, G. A. Naberezhnykh, G. N. Likhatskaya, S. D. Anastiuk, O. V. Chernikov & T. F. Solov’eva

  2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117991, Moscow, Russia

    R. H. Ziganshin

  3. Institute for Automation and Control Processes, Far East Division of the Russian Academy of Sciences, ul. Radio 5, 690041, Vladivostok, Russia

    E. V. Trifonov

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  1. E. V. Sidorin
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  2. R. H. Ziganshin
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  3. G. A. Naberezhnykh
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  4. G. N. Likhatskaya
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  5. E. V. Trifonov
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  6. S. D. Anastiuk
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  7. O. V. Chernikov
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  8. T. F. Solov’eva
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Correspondence to E. V. Sidorin.

Additional information

Original Russian Text © E. V. Sidorin, R. H. Ziganshin, G. A. Naberezhnykh, G. N. Likhatskaya, E. V. Trifonov, S. D. Anastiuk, O. V. Chernikov, T. F. Solov’eva, 2009, published in Biokhimiya, 2009, Vol. 74, No. 4, pp. 501–514.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM08-262, February 8, 2009.

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Sidorin, E.V., Ziganshin, R.H., Naberezhnykh, G.A. et al. Chaperone Skp from Yersinia pseudotuberculosis exhibits immunoglobulin G binding ability. Biochemistry Moscow 74, 406–415 (2009). https://doi.org/10.1134/S0006297909040087

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