Omp85 proteins ofNeisseria gonorrhoeaeandNeisseria meningitidisare similar toHaemophilus influenzaeD-15-Ag andPasteurella multocidaOma87

Manning, D S; Reschke, Dennis; Judd, Ralph C.

doi:10.1006/mpat.1998.0206

Cited by 43 publications

(18 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example: FetA was also identified in bands 7, 8 and 9; PorA in bands 16, 17, 18, 26, 28 and 29 and PorB in bands 14,15,16,17,18,20,24, 26 and 28. Other well documented membrane proteins identified included: Tbp1 (band 1), HmbR (band 3), TonB dependant receptors (bands 2, 3, 4 and 11) and PilQ (band 4).…”

Section: Resultsmentioning

confidence: 99%

“…It is therefore essential that manufacturers maintain growth conditions between batches to keep their products consistent with those shown to be effective in clinical studies. Key proteins present in OMVs that are thought to have an important impact on protective immunity include: Omp85, 14 FetA, 15,16 PorA, 11 PorB, 17,18 RmpM, 19 OpcA 11 and NspA. 20 Currently, demonstration of the presence of these antigens in OMV vaccines is by one-dimensional (1-D) polyacrylamide gel electrophoresis (PAGE) in the presence of sodium dodecyl sulphate (SDS) and immunoblotting with monoclonal antibodies.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterisation of the Protein Content of a Meningococcal Outer Membrane Vesicle Vaccine by Polyacrylamide Gel Electrophoresis and Mass Spectrometry

Vipond

Wheeler²,

Jones³

et al. 2005

Human Vaccines

View full text Add to dashboard Cite

Previously published online as a Human Vaccines ACKNOWLEDGEMENTSWe wish to thank Philipp Oster for critical reading of the manuscript. Research Paper Characterization of the Protein Content of a Meningococcal Outer Membrane Vesicle Vaccine by Polyacrylamide Gel Electrophoresis and Mass Spectrometry ABSTRACTThe development and evaluation of outer membrane vesicles as vaccines against meningococcal disease has been carried out for more than two decades. Although such vaccines have limitations and are not widely licensed, they continue to be used to disrupt clonal outbreaks caused by group B meningococci and a wealth of information is now available from large-scale clinical studies. One dimensional polyacrylamide gel electrophoresis and semi-quantitative measurement of the major proteins is one method used to evaluate and control these products. However, it is often difficult to determine exactly which bands on a one dimensional gel correspond to the key antigens whose presence must be demonstrated for control and lot release. We have therefore carried out mass spectrometric analyses of outer membrane vesicle vaccine samples to definitively identify the bands containing seven key antigens: Omp85, FetA, PorA, PorB, RmpM, OpcA and NspA. An additional 33 proteins present in the vaccine were also identified and this information will be useful both for future quality control and for the interpretation of data from vaccine trials.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterisation of the Protein Content of a Meningococcal Outer Membrane Vesicle Vaccine by Polyacrylamide Gel Electrophoresis and Mass Spectrometry

Vipond

Wheeler²,

Jones³

et al. 2005

Human Vaccines

View full text Add to dashboard Cite

show abstract

“…Non-denaturing SDS-PAGE (Voulhoux et al, 2003) and cross-linking experiments (Manning et al, 1998) indicated that Omp85 is part of a multi-subunit complex in N. meningitidis. These results were confirmed in E. coli, where the Omp85 homologue is now called BamA (Bam stands for b-barrel assembly machinery).…”

Section: The Bacterial Omp Assembly Machinerymentioning

confidence: 99%

Assembly of outer-membrane proteins in bacteria and mitochondria

Tommassen

2010

Microbiology

101

View full text Add to dashboard Cite

The cell envelope of Gram-negative bacteria consists of two membranes separated by the periplasm. In contrast with most integral membrane proteins, which span the membrane in the form of hydrophobic a-helices, integral outer-membrane proteins (OMPs) form b-barrels. Similar b-barrel proteins are found in the outer membranes of mitochondria and chloroplasts, probably reflecting the endosymbiont origin of these eukaryotic cell organelles. How these b-barrel proteins are assembled into the outer membrane has remained enigmatic for a long time. In recent years, much progress has been reached in this field by the identification of the components of the OMP assembly machinery. The central component of this machinery, called Omp85 or BamA, is an essential and highly conserved bacterial protein that recognizes a signature sequence at the C terminus of its substrate OMPs. A homologue of this protein is also found in mitochondria, where it is required for the assembly of b-barrel proteins into the outer membrane as well. Although accessory components of the machineries are different between bacteria and mitochondria, a mitochondrial b-barrel OMP can be assembled into the bacterial outer membrane and, vice versa, bacterial OMPs expressed in yeast are assembled into the mitochondrial outer membrane. These observations indicate that the basic mechanism of OMP assembly is evolutionarily highly conserved.

show abstract

“…Refs. [12][13][14] and BamA from Escherichia coli (formerly named YaeT) (15)(16)(17), as well as Omp85 proteins from cyanobacteria like Synechocystis (18,19) and Anabaena (20 -22).…”

mentioning

confidence: 99%

Conserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85

Koenig

Mirus²,

Haarmann³

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

Proteins of the Omp85 family are conserved in all kingdoms of life. They mediate protein transport across or protein insertion into membranes and reside in the outer membranes of Gramnegative bacteria, mitochondria, and chloroplasts. Omp85 proteins contain a C-terminal transmembrane ␤-barrel and a soluble N terminus with a varying number of polypeptide-transport-associated or POTRA domains. Here we investigate Omp85 from the cyanobacterium Anabaena sp. PCC 7120. The crystallographic three-dimensional structure of the N-terminal region shows three POTRA domains, here named P1 to P3 from the N terminus. Molecular dynamics simulations revealed a hinge between P1 and P2 but in contrast show that P2 and P3 are fixed in orientation. The P2-P3 arrangement is identical as seen for the POTRA domains from proteobacterial FhaC, suggesting this orientation is a conserved feature. Furthermore, we define interfaces for protein-protein interaction in P1 and P2. P3 possesses an extended loop unique to cyanobacteria and plantae, which influences pore properties as shown by deletion. It now becomes clear how variations in structure of individual POTRA domains, as well as the different number of POTRA domains with both rigid and flexible connections make the N termini of Omp85 proteins versatile adaptors for a plentitude of functions.Membrane proteins of the ␤-barrel type are pore proteins made up from a varying number of ␤-strands crossing the membrane. They are found exclusively in the outer membranes of bacteria, mitochondria, and chloroplasts (1). Specialized ␤-barrel proteins are involved in protein transport, called polypeptide-transporting ␤-barrel proteins (PTBs). 4 They can be divided into two classes according to their function (2-4). Class I PTBs are involved in transport of proteins from the periplasm to the extracellular space over the outer bacterial membrane. An example is the FhaC protein from Bordetella pertussis, belonging to the two-partner secretion system (4), which is required for transport of filamentous hemagglutinin. Class II proteins were initially discovered as surface-exposed antigens D15 and Oma87 from Haemophilus influenza (5, 6) and are now known to catalyze insertion of ␤-barrel proteins into the outer membrane (7-11). Analyzed members of this class include proteobacterial Omp85 proteins from Neisseria meningitidis (e.g. Refs. 12-14) and BamA from Escherichia coli (formerly named YaeT) (15-17), as well as Omp85 proteins from cyanobacteria like Synechocystis (18,19) and Anabaena (20 -22).All PTBs share a common structure with a C-terminal ␤-barrel domain, forming a membrane pore and a soluble N-terminal region. The N terminus contains a varying number of so-called polypeptide transport-associated or POTRA domains: class I PTBs have two, class II PTB one to six POTRA domains (Table 1) (15,23). The class I PTB FhaC from B. pertussis is known by crystallographic three-dimensional structure determination to comprise two POTRA domains and a 16-stranded ␤-barrel (24). For class II proteins, structural inf...

show abstract

Omp85 proteins ofNeisseria gonorrhoeaeandNeisseria meningitidisare similar toHaemophilus influenzaeD-15-Ag andPasteurella multocidaOma87

Cited by 43 publications

References 20 publications

Characterisation of the Protein Content of a Meningococcal Outer Membrane Vesicle Vaccine by Polyacrylamide Gel Electrophoresis and Mass Spectrometry

Characterisation of the Protein Content of a Meningococcal Outer Membrane Vesicle Vaccine by Polyacrylamide Gel Electrophoresis and Mass Spectrometry

Assembly of outer-membrane proteins in bacteria and mitochondria

Conserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85

Contact Info

Product

Resources

About