Levels of Serum Immunoglobulin G Specific to Bacterial Surface Protein A ofTannerella forsythiaare Related to Periodontal Status

ABSTRACT Streptococcus pneumoniae is the primary etiological agent of community-acquired pneumonia and a major cause of meningitis and bacteremia. Three conserved pneumococcal proteins—pneumolysin, pneumococcal surface adhesin A (PsaA), and pneumococcal surface protein A (PspA)—are currently being investigated as vaccine candidates. Such protein-based vaccines, if proven effective, could provide a cheaper alternative to conjugate vaccine formulae. Few data from sub-Saharan Africa exist concerning the development of natural antibody to these antigens, however. To investigate the age-specific development of antiprotein immunoglobulin G (IgG) and IgA antibody responses, the sera of 220 persons 2 weeks to 84 years of age from coastal Kenya were assayed using enzyme-linked immunosorbent assays. IgG and IgA antibody responses to each antigen were observed in all age groups. Serum concentrations of IgG and IgA antibody responses to PspA and PdB (a recombinant toxoid derivative of pneumolysin), but not to PsaA, increased significantly with age (P < 0.001). No decline was observed in the sera of the elderly. Anti-protein IgG concentrations were only weakly correlated (0.30 < r < 0.56; P < 0.0001), as were IgA concentrations (0.24 < r < 0.54; P < 0.0001).

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The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein fromClostridium difficile

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s1399004714009997 ◽

2014 ◽

Vol 70 (7) ◽

pp. 1983-1993 ◽

Cited By ~ 11

Author(s):

William J. Bradshaw ◽

Jonathan M. Kirby ◽

Nethaji Thiyagarajan ◽

Christopher J. Chambers ◽

Abigail H. Davies ◽

...

Keyword(s):

Surface Layer ◽

Cysteine Protease ◽

Cathepsin L ◽

Protein A ◽

Surface Protein ◽

Carbohydrate Binding ◽

Amino Acid Residues ◽

Strong Base ◽

Bacterial Surface ◽

Single Polypeptide

Clostridium difficileis a major problem as an aetiological agent for antibiotic-associated diarrhoea. The mechanism by which the bacterium colonizes the gut during infection is poorly understood, but undoubtedly involves a myriad of components present on the bacterial surface. The mechanism ofC. difficilesurface-layer (S-layer) biogenesis is also largely unknown but involves the post-translational cleavage of a single polypeptide (surface-layer protein A; SlpA) into low- and high-molecular-weight subunits by Cwp84, a surface-located cysteine protease. Here, the first crystal structure of the surface protein Cwp84 is described at 1.4 Å resolution and the key structural components are identified. The truncated Cwp84 active-site mutant (amino-acid residues 33–497; C116A) exhibits three regions: a cleavable propeptide and a cysteine protease domain which exhibits a cathepsin L-like fold followed by a newly identified putative carbohydrate-binding domain with a bound calcium ion, which is referred to here as a lectin-like domain. This study thus provides the first structural insights into Cwp84 and a strong base to elucidate its role in theC. difficileS-layer maturation mechanism.

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Enhanced quantification of serum immunoglobulin G from a non-model wildlife species, the Steller sea lion (Eumetopias jubatus), using a protein A ELISA

Journal of Immunological Methods ◽

10.1016/j.jim.2018.08.004 ◽

2018 ◽

Vol 462 ◽

pp. 42-47 ◽

Cited By ~ 1

Author(s):

Stephanie N. Kennedy ◽

Brittany Wilhite ◽

J. Margaret Castellini ◽

Lorrie D. Rea ◽

Thomas B. Kuhn ◽

...

Keyword(s):

Immunoglobulin G ◽

Protein A ◽

Serum Immunoglobulin ◽

Steller Sea Lion ◽

Eumetopias Jubatus ◽

Sea Lion ◽

Wildlife Species

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Modular Arrangement of Allelic Variants Explains the Divergence in Moraxella catarrhalis UspA Protein Function

Infection and Immunity ◽

10.1128/iai.00573-08 ◽

2008 ◽

Vol 76 (11) ◽

pp. 5330-5340 ◽

Cited By ~ 23

Author(s):

Michael J. Brooks ◽

Jennifer L. Sedillo ◽

Nikki Wagner ◽

Cassie A. Laurence ◽

Wei Wang ◽

...

Keyword(s):

Electron Microscopy ◽

Protein Function ◽

Moraxella Catarrhalis ◽

Protein A ◽

Surface Protein ◽

Amino Acid Sequences ◽

Peptide Sequence ◽

Allelic Variants ◽

Bacterial Surface ◽

Transmission Electron

ABSTRACT Ubiquitous surface protein A molecules (UspAs) of Moraxella catarrhalis are large, nonfimbrial, autotransporter proteins that can be visualized as a “fuzzy” layer on the bacterial surface by transmission electron microscopy. Previous studies attributed a wide array of functions and binding activities to the closely related UspA1, UspA2, and/or UspA2H protein, yet the molecular and phylogenetic relationships among these activities remain largely unexplored. To address this issue, we determined the nucleotide sequence of the uspA1 genes from a variety of independent M. catarrhalis isolates and compared the deduced amino acid sequences to those of the previously characterized UspA1, UspA2, and UspA2H proteins. Rather than being conserved proteins, we observed a striking divergence of individual UspA1, UspA2, and UspA2H proteins resulting from the modular assortment of unrelated “cassettes” of peptide sequence. The exchange of certain variant cassettes correlates with strain-specific differences in UspA protein function and confers differing phenotypes upon these mucosal surface pathogens.

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Seroepidemiological analysis of anti-pneumococcal surface protein A (PspA) immunoglobulin G by clades in Japanese population

Vaccine ◽

10.1016/j.vaccine.2020.09.068 ◽

2020 ◽

Vol 38 (47) ◽

pp. 7479-7484

Author(s):

Saeko Morino ◽

Etsuko Kitagami ◽

Hiroki Nakayama ◽

Yuka Koizumi ◽

Keiko Tanaka-Taya ◽

...

Keyword(s):

Immunoglobulin G ◽

Japanese Population ◽

Protein A ◽

Surface Protein ◽

Pneumococcal Surface Protein A

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PspA Protects Streptococcus pneumoniae from Killing by Apolactoferrin, and Antibody to PspA Enhances Killing of Pneumococci by Apolactoferrin

Infection and Immunity ◽

10.1128/iai.72.9.5031-5040.2004 ◽

2004 ◽

Vol 72 (9) ◽

pp. 5031-5040 ◽

Cited By ~ 117

Author(s):

Mirza Shaper ◽

Susan K. Hollingshead ◽

William H. Benjamin ◽

David E. Briles

Keyword(s):

Streptococcus Pneumoniae ◽

Amino Acid ◽

Active Site ◽

Protein A ◽

Surface Protein ◽

Significant Protection ◽

Bacterial Surface ◽

Amino Acid Peptide ◽

Acid Fragment ◽

Different Strains

ABSTRACT Lactoferrin is an important component of innate immunity through its sequestration of iron, bactericidal activity, and immune modulatory activity. Apolactoferrin (ALF) is the iron-depleted form of lactoferrin and is bactericidal against pneumococci and several other species of bacteria. We observed that lactoferricin (LFN), an 11-amino-acid peptide from the N terminus of lactoferrin, is bactericidal for Streptococcus pneumoniae. Strains of S. pneumoniae varied in their susceptibility to ALF. Lactoferrin is bound to the pneumococcal surface by pneumococcal surface protein A (PspA). Using mutant PspA− pneumococci of four different strains, we observed that PspA offers significant protection against killing by ALF. Knockout mutations in genes for two other choline-binding proteins (PspC and PcpA) did not affect killing by ALF. PspA did not have to be attached to the bacterial surface to inhibit killing, because the soluble recombinant N-terminal half of PspA could prevent killing by both ALF and LFN. An 11-amino-acid fragment of PspA was also able to reduce the killing by LFN. Antibody to PspA enhanced killing by lactoferrin. These findings suggested that the binding of ALF to PspA probably blocks the active site(s) of ALF that is responsible for killing.

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Human kininogens interact with M protein, a bacterial surface protein and virulence determinant

Biochemical Journal ◽

10.1042/bj3050173 ◽

1995 ◽

Vol 305 (1) ◽

pp. 173-180 ◽

Cited By ~ 50

Author(s):

A Ben Nasr ◽

H Herwald ◽

W Müller-Esterl ◽

L Björck

Keyword(s):

Molecular Weight ◽

Binding Site ◽

Clinical Medicine ◽

Protein A ◽

Surface Protein ◽

Surface Proteins ◽

M Protein ◽

Terminal Portion ◽

Bacterial Surface ◽

M1 Protein

Streptococcus pyogenes, the most significant streptococcal species in clinical medicine, expresses surface proteins with affinity for several human plasma proteins. Here we report that kininogens, the precursors to the vasoactive kinins, bind to the surface of S. pyogenes. M protein, a surface molecule and a major virulence factor-in these bacteria, occurs in > 80 different serotypes. Among 49 strains of S. pyogenes, all of different M serotypes, 41 bound radiolabelled kininogens, whereas 6 M protein-negative mutant strains showed no affinity. M protein of most serotypes bind fibrinogen, and among the 55 strains tested, binding of kininogens was closely correlated to fibrinogen binding (r = 0.88, P < 0.0001). Western blotting, slot binding and enzyme immunoassay experiments demonstrated that M proteins isolated from S. pyogenes of three different M protein serotypes (M1, M6 and M46) bound kininogens. The affinity between kininogens and M1 protein was determined to be 5 x 10(7) M-1 and < or = 10(6) M-1 for high molecular weight (H-kininogen) and low molecular weight kininogen, respectively. The kininogen binding site was tentatively mapped to the N-terminal portion of M1 protein, and this site does not overlap the specific and separate binding sites for albumin, IgG and fibrinogen using monoclonal antibodies to, and synthetic peptides of, the kininogen sequence, the major M protein-binding site(s) was mapped to the C-terminal portion of the H-kininogen light chain. We anticipate that the kininogen-M protein interaction contributes to the host-parasite relationship in S. pyogenes infections.

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Use of Protein a Conjugated to Peroxidase to Localize Immunoglobulin G in SSPE Ferret Brain

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100054376 ◽

1982 ◽

Vol 40 ◽

pp. 350-351

Author(s):

Hannah R. Brown ◽

Anthony F. Nostro ◽

Halldor Thormar

Keyword(s):

Immunoglobulin G ◽

Human Disease ◽

Measles Virus ◽

Subacute Sclerosing Panencephalitis ◽

Protein A ◽

Inflammatory Lesions ◽

Sspe Virus ◽

Specific Immunoglobulin ◽

Antibody Titers ◽

The Brain

Subacute sclerosing panencephalitis (SSPE) is a slowly progressing disease of the CNS in children which is caused by measles virus. Ferrets immunized with measles virus prior to inoculation with the cell associated, syncytiogenic D.R. strain of SSPE virus exhibit characteristics very similar to the human disease. Measles virus nucleocapsids are present, high measles antibody titers are found in the sera and inflammatory lesions are prominent in the brains. Measles virus specific immunoglobulin G (IgG) is present in the brain,and IgG/ albumin ratios indicate that the antibodies are synthesized within the CNS.

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