scholarly journals THE USE OF PRECIPITIN ANALYSIS IN AGAR FOR THE STUDY OF HUMAN STREPTOCOCCAL INFECTIONS

1958 ◽  
Vol 108 (3) ◽  
pp. 385-410 ◽  
Author(s):  
Seymour P. Halbert
Keyword(s):  
Gamma Globulin ◽  
Group A Streptococcus ◽  
Streptococcal Infections ◽  
High Potency ◽  
Streptolysin O ◽  
Combined Use ◽  
Group A ◽  
Human Gamma Globulin ◽  
Human Infections

As evidenced by precipitin analysis with pooled human gamma globulin, at least 12 distinct antigens were produced in cultures by one strain of Group A streptococcus (C203S). It was suggested on this basis, that these antigens were produced in vivo during human infections. By the combined use of continuous flow electrophoresis on paper curtains, and column chromatography with calcium phosphate gels, five of these have been isolated in a probable high state of purity. One of the components was obtained from culture filtrates of a Group C streptococcal strain. Three of the purified antigens have been tentatively identified as streptolysin "O", diphosphopyridinenucleotidase, and proteinase precursor. The latter could be very readily crystallized, and appears "identical" with that described by Elliott. The DPNase was of extremely high potency, 1 mg. being capable of destroying 12.6 gm. of DPN in 7½ minutes at 37°C. The identity of the other two components is uncertain as yet. They are distinct from each other and the above products immunologically, and are not related to the "C" carbohydrate. The applicability of these methods for the analysis of infectious diseases generally was discussed.

scholarly journals THE ANALYSIS OF STREPTOCOCCAL INFECTIONS

1961 ◽  
Vol 113 (4) ◽  
pp. 759-784 ◽  
Author(s):  
S. P. Halbert ◽  
R. Bircher ◽  
E. Dahle
Keyword(s):  
Gamma Globulin ◽  
Streptococcal Infections ◽  
Streptolysin O ◽  
Group A ◽  
Streptococcal Antigens ◽  
Electrocardiographic Changes ◽  
Human Gamma Globulin ◽  
Streptococcal Proteinase ◽  
Electrocardiographic Abnormalities

1. The rapid death which occurred after intravenous injection of activated streptolysin O from. Group A or Group C streptococci was always preceded by profound electrocardiographic alterations. After several multiples of the LD50 doses, cardiac electrical arrest or fibrillation could occur within 2 to 4 seconds after completion of the injection. 2. The streptolysin O preparations used were rather highly purified, but were known to be contaminated with small amounts of one or two other immunologically distinct components. Evidence that the observed results were due to streptolysin O was obtained by tests of the reversibly oxidized materials, and by cholesterol inactivation, as well as by in vivo protection with human gamma globulin rich in antistreptolysin antibodies. 3. Four non-streptolysin streptococcal antigens, partially or highly purified, failed to produce similar electrocardiographic changes, and were much less toxic. One of these was 3 X recrystallized and 1 X rechromatographed streptococcal proteinase. Shigella paradysenteriae type III endotoxin also did not produce striking electrocardiographic abnormalities. 4. A working hypothesis has been developed implicating streptolysin O as the etiological streptococcal factor responsible for the pathogenesis of rheumatic fever, which seems to account for the principal features of this illness.

scholarly journals THE ANALYSIS OF STREPTOCOCCAL INFECTIONS

1961 ◽  
Vol 113 (6) ◽  
pp. 1013-1028 ◽  
Author(s):  
Seymour P. Halbert ◽  
Suzanne L. Keatinge
Keyword(s):  
Rheumatic Fever ◽  
Gamma Globulin ◽  
Human Tissues ◽  
Group A Streptococci ◽  
Streptococcal Infections ◽  
Naturally Occurring ◽  
Group A ◽  
Streptococcal Antigens ◽  
Human Gamma Globulin ◽  
Naturally Occurring Antibodies

It has been found by immunoelectrophoresis, that Group A streptococci release at least 20 distinct extracellular antigens in human tissues, as judged by naturally occurring antibodies present in normal pooled human gamma globulin. Several of these precipitin arcs have been identified with streptococcal antigens previously purified by electrophoresis and chromatography. Human gamma globulin, as well as several rheumatic fever sera, were shown to be remarkably potent in antistreptococcal antibodies, when compared to four horse antibody concentrates obtained by hyperimmunization with several streptococcal filtrates. A Group C streptococcal culture concentrate revealed 8 or 9 antigens for which corresponding antibodies were present in human gamma globulin.

scholarly journals THE USE OF PRECIPITIN ANALYSIS IN AGAR FOR THE STUDY OF HUMAN STREPTOCOCCAL INFECTIONS

1955 ◽  
Vol 101 (5) ◽  
pp. 557-576 ◽  
Author(s):  
Seymour P. Halbert ◽  
Lois Swick ◽  
Constance Sonn
Keyword(s):  
Gamma Globulin ◽  
Antibody Responses ◽  
Human Antibody ◽  
Streptococcal Infections ◽  
Cell Extracts ◽  
Streptolysin O ◽  
Two Samples ◽  
Human Sera ◽  
Group A ◽  
Streptococcal Antigens

It has been shown by agar precipitin tests (Ouchterlony and Oakley) that human sera may contain from 0 to 5 antibodies against antigens present in a partially purified streptolysin O preparation, and from 0 to 7 antibodies against antigens in a crude ammonium sulfate concentrate of the streptococcal culture supernate used. These antigens were prepared from a Group A hemolytic streptococcus (strain C203S). Strong evidence was presented suggesting that some of the bands seen with streptolysin O concentrate represented antibody reponses to streptococcal antigens heretofore undescribed. Tests were also carried out with other streptococcal antigens, including streptokinase-desoxyribonuclease mixture from Group C streptococci (varidase-Lederle), crystalline proteinase, proteinase precursor, C carbohydrate, and sonic vibrated streptococcal cell extracts (group A, C203S). Fewer bands were seen with these preparations, and with some they were quite uncommon. The observations indicated that the predominating antibody responses in human streptococcal infections were to extracellular products of the micro-organisms, and only very slightly and infrequently to intracellular antigens. The human sera studied included sera from patients with active or convalescent rheumatic fever, and non-rheumatic subjects suffering from a variety of illnesses. As was expected, the rheumatic subjects showed antibody responses to many more of the antigens present in these preparations than did the nonrheumatic group. Pooled normal human gamma globulin was found to contain many of the antibodies found in potent human sera. This finding confirmed the antigen-antibody nature of the bands seen with individual sera. The epidemiological significance of these findings with gamma, globulin was briefly discussed. It was found that rabbit, guinea pig, and human antibody precipitin bands join quite readily in the Ouchterlony tests. This finding adds another tool for the identification of the precipitin bands found with human sera. Evidence was obtained which indicated differing immunological specificities of two samples of streptococcal desoxyribonuclease, one from Group A, the other from a Group C streptococcus. The value of these technics as representing a new approach to the study of human infectious disease was discussed.

scholarly journals Genome‐wide analysis of in vivo CcpA binding with and without its key co‐factor HPr in the major human pathogen group A Streptococcus

2020 ◽  
Author(s):  
Sruti DebRoy ◽  
Victor Aliaga‐Tobar ◽  
Gabriel Galvez ◽  
Srishtee Arora ◽  
Xiaowen Liang ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Human Pathogen ◽  
Genome Wide Analysis ◽  
Genome Wide ◽  
Group A

Single-chain variable fragment (scFv) targeting streptolysin O controls group A Streptococcus infection

2021 ◽  
Vol 566 ◽  
pp. 177-183
Author(s):  
Chihiro Aikawa ◽  
Kiyosumi Kawashima ◽  
Chihiro Fukuzaki ◽  
Makoto Nakakido ◽  
Kazunori Murase ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Streptolysin O ◽  
Group A

scholarly journals SpyAD, a Moonlighting Protein of Group A Streptococcus Contributing to Bacterial Division and Host Cell Adhesion

2014 ◽  
Vol 82 (7) ◽  
pp. 2890-2901 ◽  
Author(s):  
Marilena Gallotta ◽  
Giovanni Gancitano ◽  
Giampiero Pietrocola ◽  
Marirosa Mora ◽  
Alfredo Pezzicoli ◽  
...  
Keyword(s):  
Cell Division ◽  
Mammalian Cells ◽  
Group A Streptococcus ◽  
Host Cells ◽  
Knockout Mutant ◽  
Content Type ◽  
Moonlighting Protein ◽  
Group A

ABSTRACTGroup A streptococcus (GAS) is a human pathogen causing a wide repertoire of mild and severe diseases for which no vaccine is yet available. We recently reported the identification of three protein antigens that in combination conferred wide protection against GAS infection in mice. Here we focused our attention on the characterization of one of these three antigens, Spy0269, a highly conserved, surface-exposed, and immunogenic protein of unknown function. Deletion of thespy0269gene in a GAS M1 isolate resulted in very long bacterial chains, which is indicative of an impaired capacity of the knockout mutant to properly divide. Confocal microscopy and immunoprecipitation experiments demonstrated that the protein was mainly localized at the cell septum and could interactin vitrowith the cell division protein FtsZ, leading us to hypothesize that Spy0269 is a member of the GAS divisome machinery. Predicted structural domains and sequence homologies with known streptococcal adhesins suggested that this antigen could also play a role in mediating GAS interaction with host cells. This hypothesis was confirmed by showing that recombinant Spy0269 could bind to mammalian epithelial cellsin vitroand thatLactococcus lactisexpressing Spy0269 on its cell surface could adhere to mammalian cellsin vitroand to mice nasal mucosain vivo. On the basis of these data, we believe that Spy0269 is involved both in bacterial cell division and in adhesion to host cells and we propose to rename this multifunctional moonlighting protein as SpyAD (StreptococcuspyogenesAdhesion andDivision protein).

Invasive M1T1 group A Streptococcus undergoes a phase-shift in vivo to prevent proteolytic degradation of multiple virulence factors by SpeB

2003 ◽  
Vol 51 (1) ◽  
pp. 123-134 ◽  
Author(s):  
Ramy K. Aziz ◽  
Michael J. Pabst ◽  
Arthur Jeng ◽  
Rita Kansal ◽  
Donald. E. Low ◽  
...  
Keyword(s):  
Phase Shift ◽  
Virulence Factors ◽  
Group A Streptococcus ◽  
Proteolytic Degradation ◽  
Group A

An Outbreak of Fatal Nosocomial Infections Due to Group A Streptococcus on a Medical Ward

1996 ◽  
Vol 17 (7) ◽  
pp. 429-431 ◽  
Author(s):  
L. Ramage ◽  
K. Green ◽  
D. Pyskir ◽  
A.E. Simor
Keyword(s):  
Nosocomial Infections ◽  
Community Hospital ◽  
Group A Streptococcus ◽  
Hospital Setting ◽  
Streptococcal Infections ◽  
Severe Group ◽  
Life Threatening ◽  
Group A ◽  
Spread Of Infection ◽  
Dna Profiles

AbstractGroup A streptococcus is an uncommon but important cause of nosocomial infections. Outbreaks of infection most often have occurred in surgical or obstetrical patients. We describe an outbreak of severe group A streptococcal infections that occurred on a medical unit of a community hospital. Within an 8-day period, three patients developed fatal nosocomial skin and soft-tissue infection due to group A streptococcus. Three nurses who had provided care to one or more of these patients subsequently developed strepto-coccal pharyngitis, and three other nurses were treated with antibiotics for pharyngitis (cultures not obtained). Patient isolates were serotype M-nontypeable, T-11, opacity factor-positive, and shared identical DNA profiles when typed by pulsed-field gel electrophoresis; staff isolates were not available for typing. To prevent further spread of infection, the ward was closed to new admissions, and symptomatic staff were treated with antibiotics and relieved of patient-care duties. This outbreak demonstrates the ability of group A streptococcus to spread rapidly in a hospital setting and to cause severe life-threatening disease in hospitalized patients.

scholarly journals Streptococcus pyogenes evades adaptive immunity through specific IgG glycan hydrolysis

2019 ◽  
Vol 216 (7) ◽  
pp. 1615-1629 ◽  
Author(s):  
Andreas Naegeli ◽  
Eleni Bratanis ◽  
Christofer Karlsson ◽  
Oonagh Shannon ◽  
Raja Kalluru ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Vaccine Development ◽  
Group A Streptococcus ◽  
Invasive Infection ◽  
Invasive Infections ◽  
Life Threatening ◽  
Group A ◽  
Specific Igg

Streptococcus pyogenes (Group A streptococcus; GAS) is a human pathogen causing diseases from uncomplicated tonsillitis to life-threatening invasive infections. GAS secretes EndoS, an endoglycosidase that specifically cleaves the conserved N-glycan on IgG antibodies. In vitro, removal of this glycan impairs IgG effector functions, but its relevance to GAS infection in vivo is unclear. Using targeted mass spectrometry, we characterized the effects of EndoS on host IgG glycosylation during the course of infections in humans. Substantial IgG glycan hydrolysis occurred at the site of infection and systemically in the severe cases. We demonstrated decreased resistance to phagocytic killing of GAS lacking EndoS in vitro and decreased virulence in a mouse model of invasive infection. This is the first described example of specific bacterial IgG glycan hydrolysis during infection and thereby verifies the hypothesis that EndoS modifies antibodies in vivo. This mechanisms of immune evasion could have implications for treatment of severe GAS infections and for future efforts at vaccine development.

scholarly journals Group A Streptococcus AdcR Regulon Participates in Bacterial Defense against Host-Mediated Zinc Sequestration and Contributes to Virulence

2020 ◽  
Vol 88 (8) ◽  
Author(s):  
Nishanth Makthal ◽  
Hackwon Do ◽  
Brian M. Wendel ◽  
Randall J. Olsen ◽  
John D. Helmann ◽  
...  
Keyword(s):  
Pathogenic Bacteria ◽  
Group A Streptococcus ◽  
Zn Deficiency ◽  
Direct Competition ◽  
Mutant Strains ◽  
Genes Encoding ◽  
Group A ◽  
Gas Interactions

ABSTRACT Colonization by pathogenic bacteria depends on their ability to overcome host nutritional defenses and acquire nutrients. The human pathogen group A streptococcus (GAS) encounters the host defense factor calprotectin (CP) during infection. CP inhibits GAS growth in vitro by imposing zinc (Zn) limitation. However, GAS counterstrategies to combat CP-mediated Zn limitation and the in vivo relevance of CP-GAS interactions to bacterial pathogenesis remain unknown. Here, we report that GAS upregulates the AdcR regulon in response to CP-mediated Zn limitation. The AdcR regulon includes genes encoding Zn import (adcABC), Zn sparing (rpsN.2), and Zn scavenging systems (adcAII, phtD, and phtY). Each gene in the AdcR regulon contributes to GAS Zn acquisition and CP resistance. The ΔadcC and ΔrpsN.2 mutant strains were the most susceptible to CP, whereas the ΔadcA, ΔadcAII, and ΔphtD mutant strains displayed less CP sensitivity during growth in vitro. However, the ΔphtY mutant strain did not display an increased CP sensitivity. The varied sensitivity of the mutant strains to CP-mediated Zn limitation suggests distinct roles for individual AdcR regulon genes in GAS Zn acquisition. GAS upregulates the AdcR regulon during necrotizing fasciitis infection in WT mice but not in S100a9−/− mice lacking CP. This suggests that CP induces Zn deficiency in the host. Finally, consistent with the in vitro results, several of the AdcR regulon genes are critical for GAS virulence in WT mice, whereas they are dispensable for virulence in S100a9−/− mice, indicating the direct competition for Zn between CP and proteins encoded by the GAS AdcR regulon during infection.

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