Neisseria meningitidis transferrin-binding protein 1 expressed in Escherichia coli is surface exposed and binds human transferrin.

Abstract:

:A gene library of Neisseria meningitidis B15 P1.16 DNA was established in lambda Zap II and clones containing DNA encoding transferrin binding protein 1 (TBP-1) identified following hybridisation with a 63-bp DNA probe based on the codon assignment for the first 21 N-terminal amino acids of TBP-1. Sequencing of the cloned DNA demonstrated that all of the intergenic DNA (i.e. upstream of tbp-1 running through to the 3' end of the transferrin-binding protein 2 gene) and approx. 15% of tbp-1 had been cloned. The complete gene was generated using a polymerase chain reaction, with the primer for the 3' end being based on tbp-A of N. gonorrhoeae, and the approx. 2.9-kb DNA product cloned into pGem-3Z. The expressed protein (approx. 100 kDa) reacted with antiserum to an N-terminal peptide of TBP-1. In addition, the native product was surface-expressed by Escherichia coli and bound human transferrin.

journal_name

FEMS Microbiol Lett

authors

Palmer HM,Powell NB,Ala'Aldeen DA,Wilton J,Borriello SP

doi

10.1111/j.1574-6968.1993.tb06310.x

subject

Has Abstract

pub_date

1993-06-15 00:00:00

pages

139-45

issue

2

eissn

0378-1097

issn

1574-6968

journal_volume

110

pub_type

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