Trans-sialidases obtained from Trypanosoma congolense

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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C536S023100, C530S300000, C530S350000, C424S184100, C424S185100, C424S190100, C424S191100

Reexamination Certificate

active

07655784

ABSTRACT:
The invention relates to novel enzymes, which transfer sialic acid from a donor molecule onto an acceptor molecule (trans-sialidases). The enzymes are isolated from the protozoanTrypanosoma congolense. The invention also relates to functional equivalents of said enzymes, to the nucleic acid sequences and amino acid sequences that code for the enzymes and their functional equivalents, to expression constructs and vectors that contain said sequences, to recombinant microorganisms that carry the inventive coding nucleic-acid sequences, to a method for the recombinant production of the inventive enzymes, to a method for isolating said enzyme fromTrypanosoma congolense, to a method for the enzymatic sialization of acceptor molecules using the inventive enzymes, to effectors of the inventive trans-sialidases, to the use of the nucleic acid sequences, amino acid sequences, enzymes, effectors or sialization products for producing vaccines, medicaments, foodstuffs or food additives, in addition to the latter products obtained by the inventive method.

REFERENCES:
Pontes De Carvalho Lain C. et al., “Characterization of a novel trans-sialidase ofTrypanosoma bruceiprocyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor”, Journal of Experimental Medicine, vol. 177, No. 2, 1993, pp. 465-474, XP002276140.
Montagna Georgina et al., “The trans-sialidase from the African trypanosomeTrypanosoma brucei”, European Jounal of Biochemistry, vol. 269, No. 12, Jun. 2002, pp. 2941-2950, XP002276141 & Database EMBL retrieved from EBI Database accession No. AF310232, abstract.
Database EMBL XP002276142 retrieved from EBI Database accession No. AF181287, abstract.
Cremona M. L. et al., “A single tryosine differentiates active and inactiveTrypanosoma cruzitrans-sialidases”, Gene, Elsevier Biomedical Press, Amsterdam, NL, vol. 160, No. 1, Jul. 4, 1995, pp. 123-128, XP004042190 & Database EMBL retrieved from EBI Database accession No. Q26968 Trans-sialidase 45, abstract.
Tiralongo Evelin et al., “Two trans-sialidase forms with different sialic acid transfer and sialidase activites fromTrypanosoma congolense,” Journal of Biological Chemistry, vol. 278, No. 26, Jun. 27, 2003, pp. 23301-23310, XP002293242 & Databse EMBL retrieved from EBI Database accession No. Q7YZT2, Trans-Sialidase, abstract.
Engstler Markus et al., “The developmentally regulated trans-sialidase fromTrypanosoma bruceisialylates the procyclic acidic repetitive protein”, Molecular and Biochemical Parasitology, vol. 61, No. 1, 1993, pp. 1-13, XP002293243.

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