title: Sequence variability of the meningococcal lactoferrin-binding protein LbpB.
abstract: The lactoferrin receptor of Neisseria meningitidis consists of two proteins, LbpA and LbpB. LbpB is considered a promising vaccine candidate, and therefore its sequence variability was studied. LbpB from five different strains exhibited 70-80% mutual identity at the amino acid level. Most sequence variability was found in two stretches with a high content of negatively charged amino acids. These stretches were sequenced from six additional strains. One of the stretches is of variable length and is missing in some of the strains. The other stretch is present in all strains, but varies considerably in its exact amino acid sequence. The high degree of variability is disadvantageous for vaccine development, but may be useful for epidemiological studies.
authors.affiliation: Department of Molecular Cell Biology and Institute of Biomembranes, Utrecht University, 3584 CH, Utrecht, The Netherlands.
authors.forename: A
authors.initials: A
authors.lastname: Pettersson
authors.forename: J
authors.initials: J
authors.lastname: van der Biezen
authors.forename: V
authors.initials: V
authors.lastname: Joosten
authors.forename: J
authors.initials: J
authors.lastname: Hendriksen
authors.forename: J
authors.initials: J
authors.lastname: Tommassen
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D017931:DNA Primers; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D017931:DNA Primers; C027768:lactoferrin binding proteins, bacterial