Skip header and navigation

Refine By

19 records – page 1 of 2.

Agglutinins and antibodies to Francisella tularensis outer membrane antigens in the early diagnosis of disease during an outbreak of tularemia.

https://arctichealth.org/en/permalink/ahliterature38538
Source
J Clin Microbiol. 1988 Mar;26(3):433-7
Publication Type
Article
Date
Mar-1988
Author
L. Bevanger
J A Maeland
A I Naess
Author Affiliation
Department of Microbiology, Faculty of Medicine, University of Trondheim, Norway.
Source
J Clin Microbiol. 1988 Mar;26(3):433-7
Date
Mar-1988
Language
English
Geographic Location
Norway
Publication Type
Article
Keywords
Adolescent
Adult
Aged
Agglutination Tests
Agglutinins - analysis
Antibodies, Bacterial - analysis
Antigens, Bacterial - immunology
Bacterial Outer Membrane Proteins - immunology
Child
Disease Outbreaks
Enzyme-Linked Immunosorbent Assay
Francisella tularensis - immunology
Humans
Immunoassay
Immunoglobulins - immunology
Middle Aged
Norway
Tularemia - diagnosis - epidemiology - microbiology
Abstract
Tularemia was diagnosed in 57 patients during an outbreak in central Norway in 1984 and 1985. Clinical categories of the disease showed seasonal variations. A bacterial microagglutination test and an enzyme-linked immunosorbent assay (ELISA) with class-specific antibodies against Francisella tularensis outer membrane (OM) antigens were evaluated for the early diagnosis of tularemia. ELISA with immunoglobulin G (IgG), IgA, or IgM antibodies and the microagglutination test differed only marginally in diagnostic sensitivity. The OM preparation harbored F. tularensis agglutinogens and contained a variety of proteins, several of which functioned as immunogens in tularemia patients, as shown by Western blotting (immunoblotting). All 12 patients tested produced antibodies against a 43,000-molecular-weight OM protein. Individual variation was noted with regard to antibody response against other OM antigens. The OM is a suitable antigen preparation in ELISA for the diagnosis of tularemia and, presumably, contains antigens important in the immunobiology of tularemia.
PubMed ID
3356786 View in PubMed
Less detail

Biological differences in a rat insulinoma cell line obtained from different laboratories do not affect binding of human anti-islet immunoglobulins.

https://arctichealth.org/en/permalink/ahliterature26318
Source
Diabetes Res. 1986 Sep;3(7):339-44
Publication Type
Article
Date
Sep-1986
Author
R C McEvoy
B H Franklin
F. Ginsberg-Fellner
Source
Diabetes Res. 1986 Sep;3(7):339-44
Date
Sep-1986
Language
English
Publication Type
Article
Keywords
Adenoma, Islet Cell - pathology
Animals
Binding Sites, Antibody - metabolism
Cell Division
Cell Line
Comparative Study
Immunoglobulins - immunology
Insulin - secretion
Insulin Antibodies - immunology
Insulinoma - immunology - pathology - secretion
Laboratories
Mitotic Index
Pancreatic Neoplasms - immunology - pathology - secretion
Rats
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Abstract
An insulin-producing clone of rat insulinoma cells (RINm5F) has been used by several investigators as target cells for studies of both humoral and cell-mediated anti-islet immunity in diabetic animals and humans. We noted that the rate of proliferation of RINm5F cells obtained from different laboratories varied considerably, and, in the present study, we have compared the proliferation rates of RINm5F cells obtained from 3 laboratories (Uppsala, Sweden [UPP], Chicago [CHI] and New York [NY]). The cells were plated at 0.5 and 2.0 X 10(4)/cm2 and changes in cell number were measured over 5 days. Basal insulin release was also determined daily. In addition, binding of IgG from sera of human diabetics by each of the cell lines was also examined by a solid-phase, quantitative assay. Plating efficiency was significantly greater in the NY and CHI cells than UPP cells at both plating densities (p less than 0.025). When plated at 2 X 10(4)/cm2, the growth rate of the NY cells was faster than the others (NY: 100.1 +/- 7.8%/day, CHI: 72.2 +/- 8.1%/day, UPP: 78.3 +/- 14.0%/day, p less than 0.025). All growth rates were lower when cells were plated at 5 X 10(4)/cm2, and the differences in growth between the NY and the other cells was greater (NY: 94.1 +/- 12.2%/day, CHI: 61.8 +/- 5.8%/day, UPP: 58.1 +/- 5.6%/day). Insulin release also differed among the cells. More insulin was released by the NY cells than by the other cells on all days, and the CHI cells released more insulin than the UPP cells (p less than 0.01).(ABSTRACT TRUNCATED AT 250 WORDS)
PubMed ID
3022981 View in PubMed
Less detail

[Complement-binding and immuno-modulating properties of polyreactive immunoglobulins]

https://arctichealth.org/en/permalink/ahliterature57416
Source
Ukr Biokhim Zh. 2003 May-Jun;75(3):104-8
Publication Type
Article
Author
S A Bobrovnik
K A Efetov
Iu I Petrova
S V Komisarenko
Author Affiliation
Palladin Institute of Biochemistry, National Academy of Sciencis, Kyiv, Ukraine. sab@biochem.kiev.ua
Source
Ukr Biokhim Zh. 2003 May-Jun;75(3):104-8
Language
Russian
Publication Type
Article
Keywords
Adjuvants, Immunologic - metabolism
Animals
Antibodies, Monoclonal - immunology
Antibody Formation - immunology
Antigen-Antibody Reactions
Antigens - immunology
Binding, Competitive
Complement C1q - immunology - metabolism
English Abstract
Female
Immunization, Passive
Immunoglobulins - immunology - metabolism
Injections, Intravenous
Male
Mice
Mice, Inbred CBA
Abstract
New data concerning biological properties of polyreactive immunoglobulins (PRIG) were obtained as a result of treatment of mouse serum immunoglobulins by 4 M KSCN and are presented in the paper. In particular, the capacity of PRIG to bind C1q, the subunit of the first component of complement was studied. It was shown that PRIG's binding capacity to C1q is similar to that of intact immunoglobulins. Intravenous administration of PRIG into mice together with either sheep red blood cells or heat-inactivated staphylococcal bacteria did not affect the immune response to these antigens. Meanwhile, the same administration of PRIG together with the purified protein derivate of tuberculin resulted in 10-fold increase of mouse antibody response to PPD. These results demonstrate that PRIG can have some immuno-modulating properties concerning low-immunogenic antigens.
PubMed ID
14577160 View in PubMed
Less detail

Diagnostic methods for and clinical pictures of polyomavirus primary infections in children, Finland.

https://arctichealth.org/en/permalink/ahliterature258925
Source
Emerg Infect Dis. 2014 Apr;20(4):689-92
Publication Type
Article
Date
Apr-2014
Author
Tingting Chen
Laura Tanner
Ville Simell
Lea Hedman
Marjaana Mäkinen
Mohammadreza Sadeghi
Riitta Veijola
Heikki Hyöty
Jorma Ilonen
Mikael Knip
Jorma Toppari
Olli Simell
Maria Söderlund-Venermo
Klaus Hedman
Source
Emerg Infect Dis. 2014 Apr;20(4):689-92
Date
Apr-2014
Language
English
Publication Type
Article
Keywords
Adolescent
Child
Finland
Humans
Immunoglobulins - immunology
Infant
Infant, Newborn
Merkel cell polyomavirus - immunology - isolation & purification
Polyomavirus - immunology - isolation & purification
Polyomavirus Infections - diagnosis - immunology
Prospective Studies
Retrospective Studies
Tumor Virus Infections - diagnosis - immunology
Abstract
We used comprehensive serodiagnostic methods (IgM, IgG, and IgG avidity) and PCR to study Merkel cell polyomavirus and trichodysplasia spinulosa-associated polyomavirus infections in children observed from infancy to adolescence. Comparing seroconversion intervals with previous and subsequent intervals, we found that primary infections with these 2 viruses were asymptomatic in childhood.
Notes
Cites: J Clin Virol. 2011 Feb;50(2):125-921094082
Cites: Science. 2008 Feb 22;319(5866):1096-10018202256
Cites: Emerg Infect Dis. 2011 Aug;17(8):1355-6321801610
Cites: Emerg Infect Dis. 2011 Aug;17(8):1371-8021801612
Cites: J Infect Dis. 2011 Nov 15;204(10):1523-621926381
Cites: Med Microbiol Immunol. 2012 Feb;201(1):17-2321614514
Cites: Emerg Infect Dis. 2012 Feb;18(2):264-7122305021
Cites: J Clin Virol. 2012 Mar;53(3):225-3022196870
Cites: J Clin Virol. 2013 Sep;58(1):288-9123829968
Cites: J Med Virol. 1981;8(2):143-506271922
Cites: Int J Cancer. 2009 Sep 15;125(6):1250-619499548
Cites: J Clin Virol. 2010 May;48(1):44-820227338
Cites: PLoS Pathog. 2010;6(7):e100102420686659
Cites: J Infect Dis. 1983 Apr;147(4):676-846302172
Cites: J Infect Dis. 2011 Apr 15;203(8):1096-10021450999
PubMed ID
24655410 View in PubMed
Less detail

[Epidemiologic and immunologic parameters in the assessment of endemic goiter in the Orenburg region]

https://arctichealth.org/en/permalink/ahliterature32549
Source
Gig Sanit. 1998 Nov-Dec;(6):64-6
Publication Type
Article
Author
V V Utenina
A I Smoliagin
E V Popova
I V Mikhailova
N I Slepykh
Source
Gig Sanit. 1998 Nov-Dec;(6):64-6
Language
Russian
Publication Type
Article
Keywords
Adolescent
Age Factors
Antigen-Antibody Complex - immunology
Child
Child, Preschool
Comparative Study
English Abstract
Goiter, Endemic - epidemiology - immunology
Humans
Immunoglobulins - immunology
Infant
Iodine - deficiency - urine
Phagocytosis
Rosette Formation
Siberia - epidemiology
T-Lymphocytes - immunology
Abstract
Epidemiological investigations were carried out in 2328 children in the districts of the Orenburg district. Iodine deficiency was detected in the children living in the districts having low concentrations in the water and foodstuffs. There was a deviation of immunological parameters from the normal values in the children of the same districts.
PubMed ID
11013752 View in PubMed
Less detail

Erythema nodosum--a manifestation of Chlamydia pneumoniae (strain TWAR) infection.

https://arctichealth.org/en/permalink/ahliterature38287
Source
Scand J Infect Dis. 1989;21(6):693-6
Publication Type
Article
Date
1989
Author
M. Erntell
K. Ljunggren
T. Gadd
K. Persson
Author Affiliation
Department of Infectious Diseases, University Hospital, Lund, Sweden.
Source
Scand J Infect Dis. 1989;21(6):693-6
Date
1989
Language
English
Publication Type
Article
Keywords
Adolescent
Antibodies, Bacterial - immunology
Child
Chlamydia Infections - immunology
Chlamydophila psittaci - immunology - isolation & purification
Erythema Nodosum - etiology - immunology
Female
Fluorescent Antibody Technique
Humans
Immunoglobulins - immunology
Male
Sweden
Abstract
We describe 2 cases of erythema nodosum (EN) secondary to an infection with the TWAR strain of chlamydia, recently designated Chlamydia pneumoniae. Two young patients, 17 and 11 years old, were admitted with EN and no physical signs of pneumonia. One patient had a non-productive cough and fever. The other patient only ran a high fever. Chest radiography revealed bronchopneumonias. Infection with the C. pneumoniae species was proven by serologic testing using microimmunofluorescence technique. Serology and cultures for other bacteria known to induce EN were negative. Thus, C. pneumoniae (strain TWAR) can elicit EN.
PubMed ID
2694350 View in PubMed
Less detail

[Hentaxan as an immunoregulator in purulent wounds in parturient women]

https://arctichealth.org/en/permalink/ahliterature63657
Source
Lik Sprava. 2002;(2):120-3
Publication Type
Article
Date
2002
Author
A B Pryluts'ka
Source
Lik Sprava. 2002;(2):120-3
Date
2002
Language
Ukrainian
Publication Type
Article
Keywords
Adjuvants, Immunologic - therapeutic use
Adolescent
Adult
Anti-Bacterial Agents - chemistry - immunology - therapeutic use
English Abstract
Female
Gentamicins - chemistry - immunology - therapeutic use
Humans
Immunoglobulins - immunology
Obstetric Labor Complications - drug therapy - immunology
Pregnancy
Suppuration - drug therapy
T-Lymphocytes - classification - immunology
Tryptophan - chemistry - immunology
Wound Healing - immunology
Wound Infection - drug therapy - immunology
Zinc - chemistry - immunology
Abstract
Hentaxan, a new silicon sorbent, is a complex drug preparation containing hentamycin sulfate and zinc-tryptophan, endowed with antioxidant and immunomodulating activities. We used it for treating suppurating wounds in those women in labour. As many as 65 parturient women were examined. The conclusion drawn from the obtained results is that the immunomodulating potential of hentaxan is not very high, for which reason we recommend that hentaxan be combined with laferon which effects the T-link of immunity. The proposed method is at present under study.
PubMed ID
12073242 View in PubMed
Less detail

High affinity soluble ILT2 receptor: a potent inhibitor of CD8(+) T cell activation.

https://arctichealth.org/en/permalink/ahliterature101903
Source
Protein Cell. 2010 Dec;1(12):1118-27
Publication Type
Article
Date
Dec-2010
Author
Ruth K Moysey
Yi Li
Samantha J Paston
Emma E Baston
Malkit S Sami
Brian J Cameron
Jessie Gavarret
Penio Todorov
Annelise Vuidepot
Steven M Dunn
Nicholas J Pumphrey
Katherine J Adams
Fang Yuan
Rebecca E Dennis
Deborah H Sutton
Andy D Johnson
Joanna E Brewer
Rebecca Ashfield
Nikolai M Lissin
Bent K Jakobsen
Author Affiliation
Immunocore Limited, 57c Milton Park, Abingdon, Oxon, OX14 4RX, UK.
Source
Protein Cell. 2010 Dec;1(12):1118-27
Date
Dec-2010
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Antigens, CD - chemistry - genetics - pharmacology
Autoimmunity
Biological Assay
Cell Line
Cytotoxicity, Immunologic - genetics - immunology
Dose-Response Relationship, Immunologic
Humans
Immunoglobulins - immunology - metabolism
Immunologic Factors - chemistry - genetics - pharmacology
Kinetics
Lymphocyte Activation - genetics - immunology
Major Histocompatibility Complex - genetics - immunology
Molecular Sequence Data
Molecular Targeted Therapy
Mutagenesis, Site-Directed
Peptide Library
Polyethylene Glycols
Protein Binding - genetics - immunology
Receptors, Immunologic - chemistry - genetics
Recombinant Fusion Proteins - genetics - metabolism
T-Lymphocytes, Cytotoxic - immunology - metabolism
Abstract
Using directed mutagenesis and phage display on a soluble fragment of the human immunoglobulin super-family receptor ILT2 (synonyms: LIR1, MIR7, CD85j), we have selected a range of mutants with binding affinities enhanced by up to 168,000-fold towards the conserved region of major histocompatibility complex (MHC) class I molecules. Produced in a dimeric form, either by chemical cross-linking with bivalent polyethylene glycol (PEG) derivatives or as a genetic fusion with human IgG Fc-fragment, the mutants exhibited a further increase in ligand-binding strength due to the avidity effect, with resident half-times (t(1/2)) on the surface of MHC I-positive cells of many hours. The novel compounds antagonized the interaction of CD8 co-receptor with MHC I in vitro without affecting the peptide-specific binding of T-cell receptors (TCRs). In both cytokine-release assays and cell-killing experiments the engineered receptors inhibited the activation of CD8(+) cytotoxic T lymphocytes (CTLs) in the presence of their target cells, with subnanomolar potency and in a dose-dependent manner. As a selective inhibitor of CD8(+) CTL responses, the engineered high affinity ILT2 receptor presents a new tool for studying the activation mechanism of different subsets of CTLs and could have potential for the development of novel autoimmunity therapies.
PubMed ID
21213105 View in PubMed
Less detail

19 records – page 1 of 2.