Journal of Immunological Methods Impact Factor & Information

Publisher: Association of Medical Laboratory Immunologists, Elsevier

Journal description

The Journal of Immunological Methods is devoted to covering techniques for: (1) Quantitating and detecting antibodies and/or antigens and haptens based on antigen-antibody interactions. (2) Fractionating and purifying immunoglobulins, lymphokines and other molecules of the immune system. (3) Isolating antigens and other substances important in immunological processes. (4) Labelling antigens and antibodies with radioactive and other markers. (5) Localizing antigens and/or antibodies in tissues and cells, in vivo or in vitro. (6) Detecting, enumerating and fractionating immunocompetent cells. (7) Assaying for cellular immunity. (8) Detecting cell-surface antigens by cell-cell interactions. (9) Initiating immunity and unresponsiveness. (10) Transplanting tissues. (11) Studying items closely related to immunity such as complement, reticuloendothelial system and others. In addition the journal will publish articles on novel methods for analysing the organization, structure and expression of genes for immunologically important molecules such as immunoglobulins, T cell receptors and accessory molecules involved in antigen recognition, processing and presentation. Submitted full length manuscripts should describe new methods of broad applicability to immunology and not simply the application of an established method to a particular substance - although papers describing such applications may be considered for publication as a short Technical Note The Recombinant Technology section will contain articles relating to modification by recombinant techniques of molecules of immunological interest; isolation of novel binding proteins by phage display; gene therapy; transfection; and expression. Immunology Protocols is a section providing detailed, step-by-step descriptions of new and established techniques in immunology. Articles on the molecular biological analysis of immunologically relevant receptor binding sites are also invited.

Current impact factor: 2.01

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 2.005
2012 Impact Factor 2.225
2011 Impact Factor 2.203
2010 Impact Factor 2.34
2009 Impact Factor 2.347
2008 Impact Factor 2.12
2007 Impact Factor 1.947
2006 Impact Factor 2.402
2005 Impact Factor 2.572
2004 Impact Factor 2.464
2003 Impact Factor 2.744
2002 Impact Factor 2.598
2001 Impact Factor 2.283
2000 Impact Factor 1.995
1999 Impact Factor 1.95
1998 Impact Factor 1.855
1997 Impact Factor 2.043
1996 Impact Factor 1.883
1995 Impact Factor 1.901
1994 Impact Factor 2.029
1993 Impact Factor 2.104
1992 Impact Factor 1.79

Impact factor over time

Impact factor
Year

Additional details

5-year impact 2.45
Cited half-life 0.00
Immediacy index 0.50
Eigenfactor 0.01
Article influence 0.87
Website Journal of Immunological Methods website
Other titles Journal of immunological methods, Immunological methods, JIM
ISSN 0022-1759
OCLC 1783876
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Pre-print allowed on any website or open access repository
    • Voluntary deposit by author of authors post-print allowed on authors' personal website, arXiv.org or institutions open scholarly website including Institutional Repository, without embargo, where there is not a policy or mandate
    • Deposit due to Funding Body, Institutional and Governmental policy or mandate only allowed where separate agreement between repository and the publisher exists.
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months .
    • Set statement to accompany deposit
    • Published source must be acknowledged
    • Must link to journal home page or articles' DOI
    • Publisher's version/PDF cannot be used
    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • Source
    Journal of Immunological Methods 04/2015; 419. DOI:10.1016/j.jim.2015.04.003
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    ABSTRACT: Recently the analytical power of the latest high throughput next generation DNA sequencing platforms has been used to analyse phage that have been selected from the panning of large combinatorial libraries displaying either peptide or antibody ligands. This process, commonly referred to as next generation phage display (NGPD), allows the researcher to determine the identity of specific phage that are being enriched against an antigen target by analysis of the DNA sequence encoding the displayed ligand. This method bypasses several steps in conventional phage panning that include laborious colony picking and functional ligand screening. A downside of this approach is that the only output from such experiments is the DNA sequence information of such enriched phage particles. In the case of peptides, the peptide sequence can be synthesised directly and used for further screening, however this is more difficult with larger antibody fragments such as ScFvs. In the case of ScFvs, their coding sequence would have to be fully elucidated, synthesised and re-cloned before expression. We describe here the application of an inverse PCR-ligation methodology that enables the specific recovery of ScFvs of interest from enriched sub-libraries of phage clones. Phagemid particles are recovered using sequence information derived from their unique heavy chain CDR3/FR4 domains and specific clones can be recovered irrespective of CDR3 size and at levels of abundance that would be refractory to their discovery during conventional phage panning and screening. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 03/2015; DOI:10.1016/j.jim.2015.03.005
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    ABSTRACT: The study aimed to evaluate cell surface mobilisation of CD107a as a general activation marker on chicken cytotoxic T cells (CTL). Experiments comprised establishment of an in vitro model for activation induced CD107a mobilisation and design of a marker panel for detection of CD107a mobilisation on chicken CTL isolated from different tissues. Moreover, CD107a mobilisation was analysed on CTL isolated from airways of infectious bronchitis virus (IBV) infected birds direct ex vivo and upon in vitro stimulation. Results showed that phorbol 12-myristate 13-acetate (PMA) in combination with ionomycin was a consistent inducer of CD107a cell surface mobilisation on chicken CTL in a 4h cell culture model. In chickens experimentally infected with IBV, a higher frequency of CTL isolated from respiratory tissues were positive for CD107a on the cell surface compared to those from uninfected control chickens indicating in vivo activation. Moreover, upon in vitro PMA+ionomycin stimulation higher proportions of CTL isolated from the airways of IBV infected chickens showed CD107a mobilisation compared to those from uninfected control chickens. Monitoring of CD107a cell surface mobilisation may thus be a useful tool for studies of chicken CTL cytolytic potential both in vivo and in vitro. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 03/2015; 419. DOI:10.1016/j.jim.2015.02.011
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    ABSTRACT: T lymphocyte migration is crucial for adaptive immunity. Manipulation of signaling molecules controlling cell migration combined with in-vitro cell migration analysis provides a powerful research approach. Microfluidic devices, which can precisely configure chemoattractant gradients and allow quantitative single cell analysis, have been increasingly applied to cell migration and chemotaxis studies. However, there are a very limited number of published studies involving microfluidic migration analysis of genetically manipulated immune cells. In this study, we describe a simple microfluidic method for quantitative analysis of T cells expressing transfected chemokine receptors and other cell migration signaling probes. Using this method, we demonstrated chemotaxis of Jurkat transfectants expressing wild-type or C-terminus mutated CCR7 within a gradient of chemokine CCL19, and characterized the difference in transfectant migration mediated by wild-type and mutant CCR7. The EGFP-tagged CCR7 allows identification of CCR7-expressing transfectants in cell migration analysis and microscopy assessment of CCR7 dynamics. Collectively, our study demonstrated the effective use of the microfluidic method for studying CCR7 mediated T cell transfectant migration. We envision this developed method will provide a useful platform to functionally test various signaling mechanisms at the cell migration level. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; 419. DOI:10.1016/j.jim.2015.02.008
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    ABSTRACT: Bioanalytical data from early human studies conducted in normal volunteers are often used for building pharmacokinetic/pharmacodynamic models that can predict outcomes of future studies in diseased patients. Thus, it's important to develop and validate reliable and accurate bioanalytical assays that instill confidence that the intended therapeutic species (total or free) are being measured. Assays quantifying the free therapeutic species, the partially bound (for multivalent therapeutics) and unbound species, require much more characterization than assays that quantify the total therapeutic species. We have developed an immunoassay to measure free BMS-962476, an Adnectin protein therapeutic against soluble proprotein convertase subtilisin kexin (PCSK)-9, and performed an in-depth characterization of the accuracy of this assay with the assistance of modeling. The experimental data correlates with modeled data within 15% at all clinically relevant levels of PCSK9 in normal and diseased populations. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; 419. DOI:10.1016/j.jim.2015.02.009
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    ABSTRACT: The ability to avoid inflammatory responses to dietary components and microbiota antigens in the gut mucosa is achieved by a mechanism termed oral tolerance. This phenomenon is crucial to maintain the physiological immune activity in the gut and to prevent inflammatory disorders such as food allergy and inflammatory bowel diseases. Moreover, orally administered antigens induce regulatory cells that control systemic inflammatory responses as well. Given its specific, systemic and long lasting effects, oral tolerance represents a promising approach for immunotherapies that aim to modulate inflammatory and autoimmune diseases. However, there are different protocols of feeding for induction of oral tolerance and they have an impact in tolerance efficiency and length. Herein, we present and discuss different experimental feeding protocols and how they influence the outcome of oral administration of antigens. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; DOI:10.1016/j.jim.2015.02.005
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    ABSTRACT: Citrobacter rodentium is a natural mouse pathogen which reproducibly infects mice and causes intestinal disease. The C. rodentium model of infection is very useful for investigating host-pathogen immune interactions in the gut, and can also be used to understand the pathogenesis of several important human intestinal disorders, including Crohn's disease, ulcerative colitis, dysbiosis and colon tumorigenesis. Both innate and adaptive immune responses play a critical role in protection against C. rodentium. Here, we summarize the role of immune components in protection against C. rodentium and describe techniques for the analysis of innate and adaptive mucosal immune responses, including setting up the infection, analysis of colonic hyperplasia and bacterial dissemination, evaluation of antibody responses, and purification and analysis of intestinal epithelial and lymphoid cells. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; DOI:10.1016/j.jim.2015.02.003
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    ABSTRACT: Immunoconjugates that deliver cytotoxic payloads to cancer cells represent a promising class of therapeutic agents which are intensively investigated in various clinical applications. Prerequisites for the generation of effective immunoconjugates are antibodies which efficiently deliver the respective cytotoxic payload. To facilitate the selection of human or mouse antibodies that display favorable characteristics as immunotoxins, we developed a novel Pseudomonas exotoxin A (ETA)-based screening protein. The α-Fc-ETA' consists of a multispecies-specific Fc-binding domain antibody genetically fused to a truncated ETA version (ETA'). α-Fc-ETA' non-covalently bound to human and mouse antibodies but did not form immune complexes with bovine immunoglobulins. In combination with antibodies harboring human or mouse Fc domains α-Fc-ETA' inhibited proliferation of antigen-expressing tumor cells. The cytotoxic effects were strictly antibody dependent and were observed with low α-Fc-ETA' concentrations. Mouse antibodies directed against CD7 and CD317/HM1.24 that previously had been used for the generation of functional recombinant immunotoxins, also showed activity in combination with α-Fc-ETA' by inhibiting growth of antigen-positive myeloma and leukemia cell lines. In contrast, α-kappa-ETA', a similarly designed human kappa light chain-specific fusion protein, was only specifically active in combination with antibodies containing a human kappa light chain. Thus, the novel α-Fc-ETA' fusion protein is broadly applicable in screening antibodies and Fc-containing antibody derivatives from different species to select for candidates with favorable characteristics for immunotoxin development. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; DOI:10.1016/j.jim.2015.02.002
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    ABSTRACT: Specimen collection method and quality insurance is pivotal in biomarker discovery. Pre-analytical variables concerning blood collection and sample handling might affect analytical results and should be standardised prior application. In this study, we examine pre-analytical characteristics of blood samples using protein microarray. The influences of 1) standby times until centrifugation (1h, 4h, 24h and 48h), 2) four blood collection methods, and 3) IgG purified from those samples on differentially reactive antigens between samples ("DIRAGs") were investigated. Spearman correlation analyses of intra-individual arrays demonstrated remarkable differences (0.75-0.98 vs. 0.5-0.75) of antibody reactivities within and between serum and plasma samples. Class comparison showed that reactive antigen profiles were best preserved using IgG purified samples of serum tubes without separation gel as after 24hours 83% of the 1h baseline DIRAGs were re-found. Testing dilution series with protein microarrays and Luminex xMap® Technology, we found linear correlations (R(2)=0.94-0.99) between IgG concentration and read-out when using purified IgG instead of serum. Therefore, we highly recommend standardising pre-analytics and proposing the use of purified IgG for autoantibody immune-profiling with protein microarrays to reduce potential unspecific binding of matrix proteins abundant in serum and plasma samples. Although purified IgG cannot completely compensate the influence of pre-analytics, in highly parallel immune-profiling IgG enables reduction of unspecific effects, which occur when using serum or plasma for analysis on protein microarrays. Reproducibility problems due to pre-analytical processing of blood samples might explain discrepant results reported in various biomarker studies. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.009
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    ABSTRACT: Isolation and characterization of anti HIV-1 broadly neutralizing antibodies (bNAbs) has elucidated new epitopes and sites of viral vulnerability. Anti-HIV-1 bNAbs typically show high levels of somatic mutations in their variable region genes. This feature potentially limits antibody identification, since the mutated antibody sequences are no longer complimentary to primers designed based on germline antibody sequences. Here we report a new set of primers for Igλ light chains that aligns to the 5' end of the leader sequence and is highly efficient for the amplification of antibodies that contain mutations and deletions in the 5' end of human Igλ. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 02/2015; DOI:10.1016/j.jim.2015.01.011
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    ABSTRACT: The objective of this manuscript is to present an approach for evaluating specimen stability for flow cytometric methods used during drug development. While this approach specifically addresses stability assessment for assays to be used in clinical trials with centralized testing facilities, the concepts can be applied to any stability assessment for flow cytometric methods. The proposed approach is implemented during assay development and optimization, and includes suggestions for designing a stability assessment plan, data evaluation and acceptance criteria. Given that no single solution will be applicable in all scenarios, this manuscript offers the reader a roadmap for stability assessment and is intended to guide the investigator during both the method development phase and in the experimental design of the validation plan. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.008
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    ABSTRACT: Soluble Glycoprotein VI (GPVI) is an attractive marker for disorders marked by platelet activation, such as thrombotic microangiopathy, myocardial infarction, and stroke. Several groups have already developed an immunoassay for soluble GPVI; however, there are several discrepancies between the groups' assays. In this study, we prepared the two types of recombinant soluble GPVI, the monomeric form GPVI (GPVI-His) and the dimeric form of GPVI (GPVI-Fc), moreover, we generated four anti-GPVI antibodies, F1232-7-1 (7S1), F1232-10-2 (10S2), F1232-19-1 (19D1), and F1232-21-1 (21D1). The former 2 antibodies (7S1 and 10S2) had a high affinity for both GPVI-His and GPVI-Fc, while the latter 2 antibodies (19D1 and 21D1) showed a high affinity for GPVI-Fc but low affinity for GPVI-His. All of the antibodies comparably recognized surface GPVI on resting platelets. Furthermore, we established two immunoassays for soluble GPVI, 7S1/10S2-HRP and 19D1/21D1-HRP (capture antibody/detection antibody). 7S1/10S2-HRP showed equivalent reactivity with GPVI-His and GPVI-Fc, whereas 19D1/21D1-HRP had high affinity for GPVI-Fc but low reactivity with GPVI-His. In terms of reactivity with platelet-derived soluble GPVI, 7S1/10S2-HRP demonstrated sensitive detection whereas 19D1/21D1-HRP was nonreactive. Taken together, 7S1/10S2-HRP is a suitable candidate for a reliable soluble GPVI immunoassay as it has a high affinity for monomeric GPVI.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.010
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    ABSTRACT: Mesenchymal stromal cells in lymphoid organs, also called lymphoid stromal cells (LSCs), play a pivotal role in immunity by forming specialized microenvironments that provide signals for leukocyte migration, positioning, and survival. Best characterized in lymphoid organs, LSCs are also abundant in the intestinal mucosa, which harbors a rich repertoire of immune cells. However, the lack of efficient procedures for isolation and purification of LSCs from the intestine has been a major limitation to their characterization. Here we report a new method to efficiently isolate, in addition to immune cells, viable lymphoid stromal cells and other stromal subsets from the intestinal lamina propria for subsequent phenotypic and functional analysis. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 01/2015; DOI:10.1016/j.jim.2014.11.013
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    ABSTRACT: There is much debate in the pharmaceutical industry on how to translate the current guidelines on immunogenicity testing for biotherapeutics into a testing strategy that suits the specific requirements of individual drug candidates. In this paper, member companies from the European immunogenicity platform (EIP) present a consensus view on the essential requirements for immunogenicity testing of a biotherapeutic throughout the various phases of drug development, to ensure patient safety and to enable successful market entry. Our aim is to open the debate and provoke discussion on this important topic which is unique to biotherapeutic drug development. The scope of this paper is limited to aspects relevant to biotherapeutic drug development and does not include fundamental academic studies of immunogenicity. Here, we propose two pre-defined testing strategies for the detection and characterization of anti-drug antibody (ADA) responses where the different strategies are based on the phase of development for a biotherapeutic, a. without (category 1) and b. with (category 2) the expected potential to elicit ADA mediated severe clinical consequences. The harm of a potential ADA response determines which of the two testing strategies is adopted. Rather than replacing the overall risk assessment which is known to be challenging and multi-factorial, the testing strategy selection is a starting point for immunogenicity testing which adapts throughout drug development as more information becomes available. The scientific rationale on which the "case-by-case" approach advocated in white papers and guidance documents may be translated for each individual drug development program is provided and, underpins the recommendations made here. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 01/2015; 417. DOI:10.1016/j.jim.2015.01.003
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    ABSTRACT: Murine adoptive CD8+ T-cell immunotherapy studies require the generation of large numbers of high viability CD8+ cells. Here we report a tissue culture protocol for the reliable expansion of CD8+ T-cells derived from murine spleen to give a 20-fold expansion after 4days in culture. The cells were transfected with an mRNA GFP construct and transferred into NOD mice. GFP positive cells could be detected 7days after transfer thus confirming that the cells survive and are functional for up to 1week. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 01/2015; 417. DOI:10.1016/j.jim.2015.01.004
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    ABSTRACT: Skin wound healing models can be used to detect changes in immune function in response to interventions. This study used a test-retest format to assess the reliability of a skin suction blister procedure for quantitatively evaluating human immune function in repeated measures type studies. Up to eight suction blisters (~30 mm(2)) were induced via suction on each participant's left and right forearm (randomized order; blister session 1 and 2), separated by approximately one week. Fluid was sampled from each blister, and the top layer of each blister was removed to reveal up to eight skin wounds. Fluid from each wound was collected 4, 7 and 24 hours after blisters were induced, and proinflammatory cytokines were measured. Transepidermal water loss (TEWL), to assess skin barrier recovery, was measured daily at each wound site until values were within 90% of baseline values (i.e., unbroken skin). Sleep, stress and inflammation (i.e., factors that affect wound healing and immune function), preceding the blister induction, were assessed via activity monitors (Actical, Philips Respironics, Murrysville, Pennsylvania), the Perceived Stress Scale (PSS) and C-reactive protein (CRP), respectively. Area-under-the-curve and TEWL, between blister session 1 and 2, were compared using Pearson correlations and partial correlations (controlling for average nightly sleep, PSS scores and CRP). The suction blister method was considered reliable for assessing immune response and skin barrier recovery if correlation coefficients reached 0.7. Volunteers (n=16; 12 M; 4 F) were 23±5 years [mean±SD]. Time to skin barrier restoration was 4.9±0.8 and 4.8±0.9 days for sessions 1 and 2, respectively. Correlation coefficients for skin barrier restoration, IL-6, IL-8 and MIP-1α were 0.9 (P<0.0001), 0.7 (P=0.008) and 0.9 (P<0.0001), respectively. When average nightly sleep, PSS scores and CRP (i.e., percent difference between sessions 1 and 2) were taken into consideration, correlations in immune response between sessions 1 and 2 were improved for IL-8 (0.8, P=0.002) and TNF-α (0.7, P=0.02). The skin suction blister method is sufficiently reliable for assessing skin barrier restoration and immune responsiveness. This data can be used to determine sample sizes for cross-sectional or repeated-measures types of studies testing the impact of various stressors on immune response, and/or the efficacy of interventions to mitigate decrements in immune response to stress. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 01/2015; 417. DOI:10.1016/j.jim.2015.01.002