Humoral opsonins of the tunicate, Pyura stolonifera

Sarina Pearce; Rebecca A. Newton; Sham V. Nair; David A. Raftos

doi:10.1016/S0145-305X(01)00011-8

Humoral opsonins of the tunicate, Pyura stolonifera

Sarina Pearce, Rebecca A. Newton, Sham V. Nair, David A. Raftos^*

^*Corresponding author for this work

Department of Biological Sciences

Research output: Contribution to journal › Article

11 Citations (Scopus)

Abstract

This study characterizes humoral opsonins from the tunicate, Pyura stolonifera. The predominant opsonic components in P. stolonifera hemolymph were found to be calcium-dependent lectins with broad carbohydrate specificities. The opsonic lectins were purified by carbohydrate affinity chromatography which eluted a complex pattern of proteins ranging in molecular mass from 80 to >200kDa. Reducing and two dimensional SDS-PAGE indicated that the diversity of mature lectins evident under non-reducing conditions resulted from the differential oligomerization of two polypeptide sub-units (35 and 22kDa). In addition to lectin-mediated opsonic activity, hemolymph was also found to contain proteolytically activated opsonins. These data suggest that multiple, possibly interactive opsonic systems co-exist in P. stolonifera.

Original language	English
Pages (from-to)	377-385
Number of pages	9
Journal	Developmental and Comparative Immunology
Volume	25
Issue number	5-6
DOIs	https://doi.org/10.1016/S0145-305X(01)00011-8
Publication status	Published - Jun 2001

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Pearce, S., Newton, R. A., Nair, S. V., & Raftos, D. A. (2001). Humoral opsonins of the tunicate, Pyura stolonifera. Developmental and Comparative Immunology, 25(5-6), 377-385. https://doi.org/10.1016/S0145-305X(01)00011-8

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abstract = "This study characterizes humoral opsonins from the tunicate, Pyura stolonifera. The predominant opsonic components in P. stolonifera hemolymph were found to be calcium-dependent lectins with broad carbohydrate specificities. The opsonic lectins were purified by carbohydrate affinity chromatography which eluted a complex pattern of proteins ranging in molecular mass from 80 to >200kDa. Reducing and two dimensional SDS-PAGE indicated that the diversity of mature lectins evident under non-reducing conditions resulted from the differential oligomerization of two polypeptide sub-units (35 and 22kDa). In addition to lectin-mediated opsonic activity, hemolymph was also found to contain proteolytically activated opsonins. These data suggest that multiple, possibly interactive opsonic systems co-exist in P. stolonifera.",

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