scholarly journals Neurovirulence of Type 1 Polioviruses Isolated from Sewage in Japan

2002 ◽  
Vol 68 (1) ◽  
pp. 138-142 ◽  
Author(s):  
Hitoshi Horie ◽  
Hiromu Yoshida ◽  
Kumiko Matsuura ◽  
Miwako Miyazawa ◽  
Yoshihiro Ota ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Restriction Enzyme ◽  
Mutant Analysis ◽  
Group Iii ◽  
Group I ◽  
Poliomyelitis Vaccine ◽  
Vaccine Type ◽  
Enzyme Cleavage ◽  
Human Sera

ABSTRACT Sixteen type 1 poliovirus strains were isolated from a sewage disposal plant located downstream of the Oyabe River in Japan between October 1993 and September 1995. The isolates were intratypically differentiated as vaccine-derived strains. Neutralizing antigenicity analysis with monoclonal antibodies and estimation of neurovirulence by mutant analysis by PCR and restriction enzyme cleavage (MAPREC) were performed for 13 type 1 strains of these isolates. The isolates were classified into three groups. Group I (five strains) had a variant type of antigenicity and neurovirulent phenotype. Group II (four strains) had the vaccine type of antigenicity and neurovirulent phenotype. Group III (four strains) had the vaccine type of antigenicity and an attenuated phenotype. Furthermore, it was demonstrated that the virulent isolates were neutralized by human sera obtained after oral poliomyelitis vaccine (OPV) administration, and the sera of rats immunized with inactivated poliovirus vaccine. Although vaccination was effective against virulent polioviruses, virulent viruses will continue to exist in the environment as long as OPV is in use.

scholarly journals IMPORTANCE OF BLOOD GROUPS IN COMPLEMENT FIXATION REACTIONS

1920 ◽  
Vol 32 (2) ◽  
pp. 159-181 ◽  
Author(s):  
William C. Williams
Keyword(s):  
Human Serum ◽  
Cell Suspension ◽  
Guinea Pigs ◽  
Complement Fixation ◽  
Blood Groups ◽  
Group Iv ◽  
Cell Suspensions ◽  
Group Iii ◽  
Group I ◽  
Human Sera

1. The presence of a natural anti-human hemolysin, only active against Group I and Group II cells, was demonstrated in over 50 guinea pigs, obtained from different sections of the surrounding country. It was shown that, in a majority of the sera tested, this hemolysin would be a contributing factor to an excess of amboceptor in the reaction, in the quantities of complement used in an antihuman complement fixation reaction. The hemolysin is specific, in as far as it can be absorbed with either Group I or Group Il cells, but cannot be absorbed with Group III or Group IV cells. 2. To determine the effect of the isohemolysins in human serum, twenty sera were tested against cell suspensions of the four human groups. Tests were also run with twenty-six human sera against all four group cell suspensions, with complement that had the natural anti-human hemolysin absorbed from it. In both experiments various degrees of hemolysis were obtained with all but two sera against cell suspensions from Groups I, II, and III, but no hemolysis was obtained with any serum against a Group IV cell suspension. 3. The importance of the human isohemolysins and the natural anti-human hemolysm in complement was demonstrated by performing complement fixation tests upon twenty-six human sera, cell suspensions of all four human groups for each serum tested being used. A marked variation in the reaction occurred with a large percentage of the sera tested. This variation in a single serum might be as great as a negative reading with Group I cells to a double plus reading with Group IV cells. 4. That the isohemolysins, alone, in human serum are of importance in the reaction was shown by running complement fixation tests upon seventeen human sera with the four group cell suspensions and complement from which the natural anti-human hemolysin had been absorbed. Results showed a much weaker reaction, in a large number of the sera, with Group I, Group II, and Group III cells than with Group IV cells. 5. Experiments to determine a relation between the human blood groups and natural anti-sheep hemolysin present in human serum gave negative results. It was shown, however, with twenty-six human sera tested against twenty-three different sheep cell suspensions that there is a wide variation in the activity of the natural anti-sheep amboceptor present in any human serum when it is tested against different sheep cell suspensions. A human serum capable of completely hemolyzing the cells of one sheep may fail to give any hemolysis whatever when tested against another sheep cell suspension. 6. Tests were made for natural anti-sheep hemolysin in guinea pig serum. The serum from sixteen different guinea pigs was tested against a total of twenty-one sheep cell suspensions. A natural anti-sheep hemolysin was present in all the guinea pigs tested against one of the sheep cell suspensions. The same guinea pigs tested against the other sheep cell suspensions failed to show any hemolysis.

scholarly journals Shedding and Reversion of Oral Polio Vaccine Type 3 in Mexican Vaccinees: Comparison of Mutant Analysis by PCR and Enzyme Cleavage to a Real-Time PCR Assay

2007 ◽  
Vol 45 (8) ◽  
pp. 2419-2425 ◽  
Author(s):  
D. Gnanashanmugam ◽  
M. S. Falkovitz-Halpern ◽  
A. Dodge ◽  
M. Fang ◽  
L. J. Wong ◽  
...  
Keyword(s):  
Real Time ◽  
Real Time Pcr ◽  
Oral Polio Vaccine ◽  
Pcr Assay ◽  
Mutant Analysis ◽  
Polio Vaccine ◽  
Vaccine Type ◽  
Enzyme Cleavage ◽  
Type 3

scholarly journals Western Blot Analysis of Leishmania infantum Antigens in Sera of Patients with Visceral Leishmaniasis

2019 ◽  
Author(s):  
Soudabeh HEIDARI ◽  
Javad GHARECHAHI ◽  
Mehdi MOHEBALI ◽  
Behnaz AKHOUNDI ◽  
Shahab MIRSHAHVALADI ◽  
...  
Keyword(s):  
Visceral Leishmaniasis ◽  
Western Blotting ◽  
Leishmania Infantum ◽  
Negative Control ◽  
Medical Sciences ◽  
Serum Samples ◽  
Group V ◽  
Group Iii ◽  
Group I ◽  
Human Sera

Background: Visceral leishmaniasis (VL) is endemic in the northwest and south of Iran. Untreated cases of VL could cause death. The aim of the present study was to evaluate the diagnostic performance of western blotting to detect a specific immunodominant proteins pattern for Leishmania infantum infection using human sera infected with VL. Methods: We studied a panel of 122 cryopreserved human serum samples from the leishmaniasis Research Laboratory, Tehran University of Medical Sciences, Tehran, Iran from 2010 to 2017. Serum samples were collected from visceral (Group I, n: 43) and cutaneous leishmaniasis (CL) (Group II, n: 8) patients, healthy individuals from endemic (Group III, n: 13) and non-endemic (Group IV, n: 16) areas for VL, and patients with other infectious diseases (Group V, n: 42). Total antigens were prepared from the Iranian strain of L. infantum promastigote form. Results: In western blotting method, 34 protein bands of 14 to 163 kDa were recognized using the sera of VL pa­tients. The polypeptide fractions with the highest frequency including 29, 51, and 62 kDa fractions were detected using 81.4%, 79%, and 81.4% of the sera, respectively. These bands were not detected using the sera of the negative control. Moreover, 19-23, 27, 31-35, 143-163, and 109 kDa fractions were detected specifically using the sera of the patients with VL. Conclusion: This technique could be a primary step for further exploration of VL immunodominant antigens for cloning (or any technique) further investigations for future planning.

scholarly journals A Panel of Monoclonal Antibodies Targeting the Rabies Virus Phosphoprotein Identifies a Highly Variable Epitope of Value for Sensitive Strain Discrimination

2000 ◽  
Vol 38 (4) ◽  
pp. 1397-1403 ◽  
Author(s):  
S. A. Nadin-Davis ◽  
M. Sheen ◽  
M. Abdel-Malik ◽  
L. Elmgren ◽  
J. Armstrong ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Rabies Virus ◽  
Fluorescent Antibody ◽  
Antibody Test ◽  
Fusion Product ◽  
Binding Assays ◽  
Group Iii ◽  
Group I ◽  
Contrast Group ◽  
A Site

A recombinant rabies virus phosphoprotein fusion product (GST-P) was used to generate a series of monoclonal antibodies (MAbs) with anti-P reactivity. Competitive binding assays classified 27 of these MAbs into four groups (I to IV), and 24 of them were deemed to recognize linear epitopes, as judged by their reaction in immunoblots. The linear epitope recognized in each case was mapped by using two series of N- and C-terminally deleted recombinant phosphoproteins. Assessment of the reactivities of representative MAbs to a variety of lyssavirus isolates by an indirect fluorescent antibody test indicated that group I MAbs, which recognized a highly conserved N-terminal epitope, were broadly cross-reactive with all lyssaviruses assayed, while group III MAbs, which reacted with a site overlapping that of group I MAbs, exhibited variable reactivities and group IV MAbs reacted with most isolates of genotypes 1, 6, and 7 only. In contrast, group II MAbs, which recognized an epitope located within a highly divergent central portion of the protein, were exquisitely strain specific. These anti-P MAbs are potentially useful tools for lyssavirus identification and discrimination.

scholarly journals Quantitative aspects of the mutant analysis by PCR and restriction enzyme cleavage (MAPREC).

1993 ◽  
Vol 3 (3) ◽  
pp. 176-180 ◽  
Author(s):  
Z Lu ◽  
M P Douthitt ◽  
R E Taffs ◽  
Y Ran ◽  
L P Norwood ◽  
...  
Keyword(s):  
Restriction Enzyme ◽  
Mutant Analysis ◽  
Enzyme Cleavage

scholarly journals Evaluation of Serum Fibrinogen, Plasminogen,α2-Anti-Plasmin, and Plasminogen Activator Inhibitor Levels (PAI) and Their Correlation with Presence of Retinopathy in Patients with Type 1 DM

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Sefika Burcak Polat ◽  
Nagihan Ugurlu ◽  
Fatma Yulek ◽  
Huseyin Simavli ◽  
Reyhan Ersoy ◽  
...  
Keyword(s):  
Plasminogen Activator Inhibitor ◽  
Group Iv ◽  
Control Group ◽  
Positive Correlation ◽  
Group Iii ◽  
Group I ◽  
And Control ◽  
Type 1 Dm ◽  
Activator Inhibitor

Background.Diabetic retinopathy (DR) is the leading cause of blindness in the world. Retinopathy can still progress despite optimal metabolic control. The aim of the study was to determine whether different degrees of DR (proliferative or nonproliferative) were associated with abnormally modulated hemostatic parameters in patients with T1DM.Method.52 T1DM patients and 40 healthy controls were enrolled in the study. Patients were subdivided into three categories. Group I was defined as those without retinopathy, group II with NPRP, and group III with PRP. We compared these subgroups with each other and the control group (Group IV) according to the serum fibrinogen, plasminogen, alpha2-anti-plasmin (α2-anti-plasmin), and PAI.Results. We detected that PAI-1, serum fibrinogen, and plasminogen levels were similar between the diabetic and control groups (P=0.209,P=0.224, andP=0.244, resp.), whereasα2-anti-plasmin was higher in Groups I, II, and III compared to the control group (P<0.01,P<0.05, andP<0.001, resp.). There was a positive correlation between serumα2-anti-plasmin and HbA1c levels (r=0,268,P=0.031).Conclusion. To our knowledge there is scarce data in the literature aboutα2-anti-plasmin levels in type 1 diabetes. A positive correlation betweenα2-anti-plasmin with HbA1c suggests that fibrinolytic markers may improve with disease regulation and better glycemic control.

scholarly journals Anti-erythropoietin receptor (EPO-R) monoclonal antibodies inhibit erythropoietin binding and neutralize bioactivity

Blood ◽  
1993 ◽  
Vol 82 (1) ◽  
pp. 46-52 ◽  
Author(s):  
AD D'Andrea ◽  
BJ Rup ◽  
MJ Fisher ◽  
S Jones
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Amino Acid Identity ◽  
Erythropoietin Receptor ◽  
Group Iii ◽  
Human Erythropoietin ◽  
Group I ◽  
Dependent Growth ◽  
The One

We have generated six high affinity monoclonal antibodies (MoAbs) to the human erythropoietin receptor (hEPO-R) polypeptide. All six MoAbs bind to the extracytoplasmic domain of the hEPO-R, and all immunoprecipitate 35S-labeled hEPO-R from metabolically labeled Ba/F3- hEPO-R cells. Four of the MoAbs neutralize the EPO-dependent growth of Ba/F3-hEPO-R cells, whereas two MoAbs are non-neutralizing. None of the MoAbs inhibit the EPO-dependent growth of Ba/F3 cells expressing the murine EPO-R (mEPO-R), even though the hEPO-R and mEPO-R share 82% amino acid identity. All six of the anti-EPO-R MoAbs bind to the cell surface human EPO-R but none bind to the cell surface murine EPO-R. Of the four neutralizing MoAbs, the one-half maximal inhibition occurs at MoAb concentrations ranging from 1 nmol/L to 50 nmol/L. These MoAbs also compete with radiolabeled EPO for hEPO-R binding. The two non- neutralizing MoAbs fail to inhibit EPO-dependent growth or compete with EPO-binding, even at antibody concentrations as high as 500 nmol/L. The four neutralizing MoAbs, designated group I, compete with each other for an epitope of the hEPO-R polypeptide required for EPO-binding. The two non-neutralizing MoAbs recognize discrete epitopes, and are designated group II and group III MoAbs. In conclusion, this is the first description of MoAbs specific for the hEPO-R. The MoAbs, which recognize three discrete epitopes, may be useful in characterizing the spectrum of cells that display the hEPO-R and in further defining the role of EPO in hematopoiesis.

scholarly journals The identification of epitopic sites in human α1-proteinase inhibitor

1987 ◽  
Vol 246 (1) ◽  
pp. 25-36 ◽  
Author(s):  
X J Zhu ◽  
S S Kang ◽  
K Hargrove ◽  
D Shochat ◽  
M Jarrells ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Proteinase Inhibitor ◽  
Polyclonal Antibodies ◽  
Amino Acid Sequences ◽  
Enzyme Linked Immunosorbent Assay ◽  
Proteolytic Digestion ◽  
Group Iii ◽  
Group I ◽  
Hybridoma Technology ◽  
Cnbr Cleavage

Human α 1-proteinase inhibitor (α 1-PI) yielded nine fragments on cleavage with CNBr. The amino acid sequences of these fragments were determined. Three of these CNBr-cleavage fragments, namely fragment I (residues 64-220), fragment II (residues 243-351) and fragment III (residues 1-63), were found to bind rabbit polyclonal antibodies against chemically oxidized α 1-PI and mouse polyclonal antibodies against native α 1-PI by the Bio-Dot method (enzyme-linked immunosorbent assay on nitrocellulose). These fragments, I, II and III, inhibited by 60%, 25% and 5% respectively the binding between α 1-PI and the rabbit antibodies. Fragments I, II and III were subjected to proteolytic digestion, and 15, ten and five peptides were obtained from these fragments respectively. Only four of these peptides showed binding to the mouse antibodies against native α 1-PI. These were residues 40-63, 79-86, 176-206 and 299-323. A panel of monoclonal antibodies was prepared by conventional hybridoma technology, with chemically oxidized α 1-PI as the antigen. The ability of the monoclonal antibodies to bind native α 1-PI and CNBr-cleavage fragments I-III was determined. The monoclonal antibodies fell into three categories. Most (over 90%) belonged to group I, which was capable of binding α 1-PI and only fragment I. Antibodies in groups II and III bound α 1-PI and either fragment II or fragment III respectively. The ability of the peptides derived from proteolytic digestion of fragments I, II and III to bind three monoclonal antibodies representing each of the three groups was determined. Among all the peptides tested, only one (residues 176-206) derived from fragment I showed binding to the antibodies from group I, one (residues 299-323) derived from fragment II showed binding to the antibodies from group II, and one (residues 40-63) from fragment III showed binding to the antibodies from group III. Each of these three peptides also inhibited the binding between α 1-PI and the corresponding monoclonal antibodies. From these data we concluded that at least four epitopic regions (residues 40-63, 79-86, 176-206 and 299-323) were present in α 1-PI. Specific monoclonal antibodies to three of these sites were obtained.

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