Maltodextrin pore proteins in the outer membrane of Escherichia coli and Klebsiella pneumoniae: Immunological comparison

Pick, Kat; Wöber, Günter

doi:10.1111/j.1574-6968.1979.tb03260.x

FEMS Microbiology Letters

1979

DOI: 10.1111/j.1574-6968.1979.tb03260.x

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Maltodextrin pore proteins in the outer membrane of Escherichia coli and Klebsiella pneumoniae: Immunological comparison

Kat Pick

Günter Wöber

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1985

1993

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Cited by 4 publications

(1 citation statement)

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“…The presence of a protein homologous to the LamB protein has already been reported in Shigella sp. (35), Salmonella typhimurium (26), and Klebsiella pneumoniae (27). We have now extended this observation to other members of the family Enterobacteriaceae and have analyzed this family of homologous proteins for the presence of six epitopes, defined by the six mAbs previously characterized in our laboratory (17,32).…”

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confidence: 88%

Antigenic polymorphism of the LamB protein among members of the family Enterobacteriaceae

Bloch¹,

Desaymard²

1985

J Bacteriol

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In this study we demonstrate that most members of the family Enterobacteriaceae possess a maltose-inducible outer membrane protein homologous to the LamB protein of Escherichia coli K-12. These proteins react with polyclonal antibodies raised against the LamB protein of E. coli K-12. We compared the antigenic structure of the LamB protein in members of the family Enterobacteriaceae with six monoclonal antibodies raised against the LamB protein ofE. coli K-12. Four of them reacted with epitopes located at the outer face of the membrane, and two reacted with epitopes located at the inner face of the membrane. A great degree of variability was observed for the external epitopes. Even in a single species, such as E. coli, an important polymorphism was present. In contrast, the internal epitopes were more conserved.

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mentioning

confidence: 88%

Antigenic polymorphism of the LamB protein among members of the family Enterobacteriaceae

Bloch¹,

Desaymard²

1985

J Bacteriol

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DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: implications for the topology and the pore functions in maltoporin

et al. 1992

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We have determined the sequence of the lamB gene from Klebsiella pneumoniae. It encodes the precursor to the LamB protein, a 429 amino acid polypeptide with maltoporin function. Comparison with the Escherichia coli LamB protein reveals a high degree of homology, with 325 residues strictly identical. The N-terminal third of the protein is the most conserved part of the molecule (1 change in the signal sequence, and 13 changes up to residue 146 of the mature protein). Differences between the two mature proteins are clustered mainly in six regions comprising residues 145-167, 173-187, 197-226, 237-300, 311-329, and 367-387 (K. pneumoniae LamB sequence). The most important changes were found in regions predicted by the two-dimensional model of LamB folding to form loops on the cell surface. In vivo maltose and maltodextrin transport properties of E. coli K12 and K. pneumoniae strains were identical. However, none of the E. coli K12 LamB-specific phages was able to plaque onto K. pneumoniae. Native K. pneumoniae LamB protein forms highly stable trimers. The protein could be purified by affinity chromatography on starch-Sepharose as efficiently as the E. coli K12 LamB protein, indicating a conservation of the binding site for dextrins. However, none of the monoclonal antibodies directed against native E. coli K12 LamB protein recognized native purified K. pneumoniae LamB protein. These data indicate that most of the variability occurs within exposed regions of the protein and provide additional support for the proposed model of LamB folding.(ABSTRACT TRUNCATED AT 250 WORDS)

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Maltoporins and maltose-binding proteins of Yersinia enterocolitica

Brzostek

Heleszko²,

Hrebenda³

1993

Journal of General Microbiology

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Maltodextrin pore proteins in the outer membrane of Escherichia coli and Klebsiella pneumoniae: Immunological comparison

Cited by 4 publications

References 18 publications

Antigenic polymorphism of the LamB protein among members of the family Enterobacteriaceae

Antigenic polymorphism of the LamB protein among members of the family Enterobacteriaceae

DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: implications for the topology and the pore functions in maltoporin

Maltoporins and maltose-binding proteins of Yersinia enterocolitica

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