The binding spectra of carp C3 isotypes against natural targets independent of the binding specificity of their thioester

Satoko Ichiki, Yoko Kato-Unoki, Tomonori Somamoto, Miki Nakao

研究成果: ジャーナルへの寄稿学術誌査読

31 被引用数 (Scopus)

抄録

The central component of complement, C3, plays a versatile role in innate immune defense of vertebrates and some invertebrates. A notable molecular characteristic of this component is an intra-chain thioester site that enables C3 to bind covalently to its target. It has been reported that the binding preference of the thioester to hydroxyl or amino groups is primarily defined by presence or absence of the catalytic histidine residue at position 1126 in human C3. In teleosts, a unique C3 (non-His type) has been found, in addition to the common His type C3. These distinct C3 isoforms may provide diversity in the target-binding attributable to the different binding specificities of their thioesters. In the present study, we examine the hypothesized correlation of the catalytic histidine with the binding spectra of two major C3 isotypes of carp towards various model and natural targets. The results reveal that non-His type C3, rather than His type C3, has a wider range of binding spectrum, despite the binding specificity of its thioester being limited to amino groups. It is therefore hypothesized that the binding spectra of C3 isotypes are not defined by the binding specificity of the thioester but is more affected by differences in microbe-associated molecular patterns that activate complement. Overall, the present data imply that non-His type C3 plays a significant role against bacterial infections in the fish defense system.

本文言語英語
ページ(範囲)10-16
ページ数7
ジャーナルDevelopmental and Comparative Immunology
38
1
DOI
出版ステータス出版済み - 9月 2012

!!!All Science Journal Classification (ASJC) codes

  • 免疫学
  • 発生生物学

フィンガープリント

「The binding spectra of carp C3 isotypes against natural targets independent of the binding specificity of their thioester」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル