The Skeletal Amino Acid Composition of the Marine Demosponge Aplysina cavernicola     

Susanne Ueberlein  Susanne Machill  Hendrik Niemann  Peter Proksch  Eike Brunner 《Marine drugs》2014,12(8):4417-4438

It has been discovered during the past few years that demosponges of the order Verongida such as Aplysina cavernicola exhibit chitin-based skeletons. Verongida sponges are well known to produce bioactive brominated tyrosine derivatives. We could recently demonstrate that brominated compounds do not exclusively occur in the cellular matrix but also in the skeletons of the marine sponges Aplysina cavernicola and Ianthella basta. Our measurements imply that these yet unknown compounds are strongly, possibly covalently bound to the sponge skeletons. In the present work, we determined the skeletal amino acid composition of the demosponge A. cavernicola especially with respect to the presence of halogenated amino acids. The investigations of the skeletons before and after MeOH extraction confirmed that only a small amount of the brominated skeleton-bound compounds dissolves in MeOH. The main part of the brominated compounds is strongly attached to the skeletons but can be extracted for example by using Ba(OH)₂. Various halogenated tyrosine derivatives were identified by GC-MS and LC-MS in these Ba(OH)₂ extracts of the skeletons.  相似文献   

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition     

Calarese DA  Scanlan CN  Zwick MB  Deechongkit S  Mimura Y  Kunert R  Zhu P  Wormald MR  Stanfield RL  Roux KH  Kelly JW  Rudd PM  Dwek RA  Katinger H  Burton DR  Wilson IA 《Science (New York, N.Y.)》2003,300(5628):2065-2071

Human antibody 2G12 neutralizes a broad range of human immunodeficiency virus type 1 (HIV-1) isolates by binding an unusually dense cluster of carbohydrate moieties on the "silent" face of the gp120 envelope glycoprotein. Crystal structures of Fab 2G12 and its complexes with the disaccharide Manalpha1-2Man and with the oligosaccharide Man9GlcNAc2 revealed that two Fabs assemble into an interlocked VH domain-swapped dimer. Further biochemical, biophysical, and mutagenesis data strongly support a Fab-dimerized antibody as the prevalent form that recognizes gp120. The extraordinary configuration of this antibody provides an extended surface, with newly described binding sites, for multivalent interaction with a conserved cluster of oligomannose type sugars on the surface of gp120. The unique interdigitation of Fab domains within an antibody uncovers a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces.  相似文献