Humoral antibody response to extracellular, intracellular and cell envelope proteins of Staphylococcus aureus in cases of staphylococcal endocarditis

1988 ◽  
Vol 16 (6) ◽  
pp. 997-998 ◽  
Author(s):  
BAHJAT S. S. AL-ANI ◽  
GEOFFREY COLEMAN
Keyword(s):  
Staphylococcus Aureus ◽  
Antibody Response ◽  
Cell Envelope ◽  
Envelope Proteins ◽  
Humoral Antibody

Humoral antibody response to cattle to formalinized Staphylococcus aureus vaccine

1975 ◽  
Vol 21 (11) ◽  
pp. 1756-1759
Author(s):  
T. K. S. Mukkur ◽  
Usha J. Tewari
Keyword(s):  
Staphylococcus Aureus ◽  
Antibody Response ◽  
Post Partum ◽  
Post Inoculation ◽  
Freund’S Complete Adjuvant ◽  
Humoral Antibody ◽  
Freund's Complete Adjuvant ◽  
Agglutination Titer

Five cows were inoculated intradermally with formalinized Staphylococcus aureus suspension in Freund's complete adjuvant and the development of the humoral antibody response was followed as judged by the agglutination titer of sera, at various intervals post inoculation. Highest titers were observed at 78–87 days post inoculation. Agglutinating activity was found in IgM and IgG fractions (IgG1 and IgG2) of both serum and colostrum. The agglutinating activity of colostrum was significantly higher at 12 than at 24 and 36 h, post partum. However, no such activity was detected in either normal cow serum or colostrum against S. aureus.

Effects of single exposure to cadmium on the primary humoral antibody response

1983 ◽  
Vol 54 (4) ◽  
pp. 289-296 ◽  
Author(s):  
R. Kawamura ◽  
F. Shimizu ◽  
H. Fujimaki ◽  
K. Kubota
Keyword(s):  
Antibody Response ◽  
Single Exposure ◽  
Humoral Antibody

Humoral Antibody Response to the Antigens of Virulent Rhodococcus equi in Foals.

1994 ◽  
Vol 5 (4) ◽  
pp. 121-126 ◽  
Author(s):  
Shinji TAKAI ◽  
Hisashi KITAJIMA ◽  
Yoshihiro TAMADA ◽  
Susumu MATSUKURA ◽  
Yasuo OHWA ◽  
...  
Keyword(s):  
Antibody Response ◽  
Rhodococcus Equi ◽  
Humoral Antibody

Immunosuppression by Murine Sarcoma Virus (Moloney)

1970 ◽  
Vol 1 (3) ◽  
pp. 288-292
Author(s):  
S. P. Chan ◽  
W. A. Hook ◽  
W. Turner ◽  
M. A. Chirigos
Keyword(s):  
Antibody Response ◽  
Survival Time ◽  
Primary Tumor ◽  
Sheep Erythrocyte ◽  
Humoral Antibody ◽  
Secondary Tumors ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Erythrocyte Antigen ◽  
Murine Sarcoma

Infection of mice with the murine sarcoma virus (Moloney) markedly suppressed the humoral antibody response to sheep erythrocyte antigen injected 10 days after infection, when tumor size was maximal, and on day 26, when primary tumors had partially regressed. Humoral antibody response was also inhibited when antigen was injected at the time secondary tumors and metastases were evident. No significant suppression of humoral antibody was seen when mice were injected with sheep erythrocyte antigen 5 days after virus infection. Inhibition of the cellular immune response of murine sarcoma virus (Moloney)-infected mice, as measured by the increased survival time of skin grafts, was also determined. Mice that were infected 5 days prior to grafting demonstrated prolonged survival of grafts, suggesting a suppression of cellular immunity. These mice had a graft survival time 14 days greater than noninfected controls. No significant prolongation of graft survival was seen in mice grafted at the times of maximum primary tumor growth, of primary tumor regression, or when secondary tumors had appeared.

scholarly journals Ginsan Enhances Humoral Antibody Response to Orally Delivered Antigen

2010 ◽  
Vol 10 (1) ◽  
pp. 5 ◽  
Author(s):  
Hee Sam Na ◽  
You Jin Lim ◽  
Yeon-Sook Yun ◽  
Mi Na Kweon ◽  
Hyun-Chul Lee
Keyword(s):  
Antibody Response ◽  
Humoral Antibody

Single-Molecule Force Spectroscopy of Microbial Cell Envelope Proteins

2011 ◽  
pp. 317-334 ◽  
Author(s):  
Claire Verbelen ◽  
Vincent Dupres ◽  
David Alsteens ◽  
Guillaume Andre ◽  
Yves Dufrêne
Keyword(s):  
Single Molecule ◽  
Cell Envelope ◽  
Force Spectroscopy ◽  
Envelope Proteins ◽  
Microbial Cell ◽  
Single Molecule Force Spectroscopy

scholarly journals Reduction of the Peptidoglycan Crosslinking Causes a Decrease in Stiffness of the Staphylococcus aureus Cell Envelope

2014 ◽  
Vol 107 (5) ◽  
pp. 1082-1089 ◽  
Author(s):  
Peter Loskill ◽  
Pedro M. Pereira ◽  
Philipp Jung ◽  
Markus Bischoff ◽  
Mathias Herrmann ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Envelope

scholarly journals Lipoprotein N-Acylation in Staphylococcus aureus Is Catalyzed by a Two-Component Acyl Transferase System

mBio ◽  
2020 ◽  
Vol 11 (4) ◽  
Author(s):  
John H. Gardiner ◽  
Gloria Komazin ◽  
Miki Matsuo ◽  
Kaitlin Cole ◽  
Friedrich Götz ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Envelope ◽  
Opportunistic Pathogen ◽  
Structural Heterogeneity ◽  
Cysteine Residue ◽  
Acyl Transfer ◽  
Acyl Transferase ◽  
Content Type ◽  
Tailoring Enzymes ◽  
And Shifts

ABSTRACT Bacterial lipoproteins (Lpps) are a class of membrane-associated proteins universally distributed among all bacteria. A characteristic N-terminal cysteine residue that is variably acylated anchors C-terminal globular domains to the extracellular surface, where they serve numerous roles, including in the capture and transport of essential nutrients. Lpps are also ligands for the Toll-like receptor 2 (TLR2) family, a key component of the innate immune system tasked with bacterial recognition. While Lpp function is conserved in all prokaryotes, structural heterogeneity in the N-terminal acylation state is widespread among Firmicutes and can differ between otherwise closely related species. In this study, we identify a novel two-gene system that directs the synthesis of N-acylated Lpps in the commensal and opportunistic pathogen subset of staphylococci. The two genes, which we have named the lipoprotein N-acylation transferase system (Lns), bear no resemblance to previously characterized N-terminal Lpp tailoring enzymes. LnsA (SAOUHSC_00822) is an NlpC/P60 superfamily enzyme, whereas LnsB (SAOHSC_02761) has remote homology to the CAAX protease and bacteriocin-processing enzyme (CPBP) family. Both LnsA and LnsB are together necessary and alone sufficient for N-acylation in Staphylococcus aureus and convert the Lpp chemotype from diacyl to triacyl when heterologously expressed in Listeria monocytogenes. Acquisition of lnsAB decreases TLR2-mediated detection of S. aureus by nearly 10-fold and shifts the activated TLR2 complex from TLR2/6 to TLR2/1. LnsAB thus has a dual role in attenuating TLR2 signaling in addition to a broader role in bacterial cell envelope physiology. IMPORTANCE Although it has long been known that S. aureus forms triacylated Lpps, a lack of homologs to known N-acylation genes found in Gram-negative bacteria has until now precluded identification of the genes responsible for this Lpp modification. Here, we demonstrate N-terminal Lpp acylation and chemotype conversion to the tri-acylated state is directed by a unique acyl transferase system encoded by two noncontiguous staphylococci genes (lnsAB). Since triacylated Lpps stimulate TLR2 more weakly than their diacylated counterparts, Lpp N-acylation is an important TLR2 immunoevasion factor for determining tolerance or nontolerance in niches such as in the skin microbiota. The discovery of the LnsAB system expands the known diversity of Lpp biosynthesis pathways and acyl transfer biochemistry in bacteria, advances our understanding of Lpp structural heterogeneity, and helps differentiate commensal and noncommensal microbiota.

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