Analyses of varicella-zoster virus (VZV) protein expression during latency have been discordant, with rare to many positive neurons detected. We show that ascites-derived murine and rabbit antibodies specific for VZV proteins in vitro contain endogenous antibodies that react with human blood type A antigens in neurons. Apparent VZV neuronal staining and blood type A were strongly associated (by a 2 test, ␣ ؍ 0.0003). Adsorption of ascites-derived monoclonal antibodies or antiserum with type A erythrocytes or the use of in vitro-derived VZV monoclonal antibodies eliminated apparent VZV staining. Animal-derived antibodies must be screened for anti-blood type A reactivity to avoid misidentification of viral proteins in the neurons of the 30 to 40% of individuals who are blood type A. V aricella-zoster virus (VZV) is a human alphaherpesvirus that establishes latency in ganglionic sensory neurons. In autopsied human ganglia, the frequency of individual VZV-positive neurons was 1.0 to 6.9% by single-cell laser capture microdissection (LCMD) and PCR (29). However, immunostaining analyses of VZV protein expression in latently infected neurons have differed significantly. Mahalingam et al. reported infrequent detection of VZV proteins in cadaver ganglia, and in positive tissues VZV protein expression was restricted to very few neurons, a finding confirmed by Kennedy et al. and our recent study (13,16,32). In contrast, Lungu et al. detected VZV proteins in 9 to 24% of neurons in ganglia from three of three subjects (15). Theil et al. found immediate-early 62 (IE62) proteins in ganglia from 38% of individuals and in 3 to 7% of neurons (25). Discrepancies among reports describing the frequencies of VZV protein-positive neurons in autopsied ganglia require further investigation because of their implications for understanding mechanisms of VZV latency.Using a high-potency rabbit anti-IE63 antibody and preimmune serum control, we detected IE63 proteins in ganglia from only 1 of 18 individuals and in Ͻ2.8% of neurons (32). Subsequently, we observed cytoplasmic immunoreactivity in many neurons in ganglia from several individuals when the neurons were stained with monoclonal antibodies (MAbs) to IE62, glycoprotein E (gE), and the capsid protein ORF40 (MAB8616, MAB8612, and MAB8614, respectively; EMD Millipore, Billerica, MA); different lots had similar reactivities. These commercial reagents against IE62 and gE, known to be specific for viral proteins in cultured cells, have been used in studies that report cytoplasmic localization of VZV proteins in neurons (6,9,10,25,26,28). The failure to confirm IE62 and gE detection with other VZV antibodies, the detection of the ORF40 capsid protein detection in latency, and the Golgi zone-like localization of all three VZV proteins suggested a possible staining artifact.The mouse ascites Golgi (MAG) reaction results from endogenous anti-human blood type A antibodies in MAbs derived from mouse ascites (2, 5, 14, 21-23, 30, 31). Importantly, in blood type A individuals, sensory neurons exp...
Histocompatibility is necessary for many collaborative and aggressive cell interactions. The sharing of alleles at certain loci of the H-2 region on chromosome 17 of the mouse is essential for optimal interaction of lymphocytes with each other (1-7), with macrophages (8, 9), and with target cells in certain types of cytotoxic killing by T lymphocytes (10)(11)(12)(13)(14)(15)(16)(17). This evidence indicates that lymphocytes can and must recognize products of the H-2-chromosomal region for optimal responses to take place.Several curious observations which bear on the general question of self-recognition by lymphocytes have appeared in the recent literature. Koskimies and M~ikel~i (18) reported that T-cell-deficient mice made stronger anti-hapten responses to conjugates of syngeneic erythrocytes than to conjugates of allogeneic or xenogeneic erythrocytes. These findings, together with others demonstrating that an appreciable fraction of murine lymphocytes form rosettes with autologous, but not with isologous, erythrocytes (19)(20), support the existence on at least some immunocytes of a receptor for a self-marker which is expressed on erythrocytes.Because this form of self-recognition is likely to be of significance for a complete understanding of the mechanisms of lymphocyte activation, it was of interest to further investigate the phenomenon of autologous rosette formation. The present study confirms the phenomenon, establishes that the receptor in question is expressed on both T and B lymphocytes, and that it is not immunoglobulin in nature. Moreover, the use of recombinant strains of mice indicates that this form of self-recognition is associated with a marker coded by a new locus in the H-2-region mapping between H-2G and H-2D.
Fetal bovine serum is in widespread use for in vitro antibody-synthesizing systems, but very little attention has been paid to the complement (C) activity of this serum, at least partly because methods have not been developed for measuring some bovine C components, particularly C3. We report here some studies on bovine C1, and a simple assay for bovine C3 and its use to measure the C3 content of a number of commercial and other fetal bovine serum preparations, which were “good” or “bad” with respect to their ability to support (in vitro antibody synthesis. The C1, C3b-inactivator and conglutinin contents of these preparations will also be reported. C1 was precipitated twice from normal bovine serum at 0.03 M NaCl and 0.005 M phosphate concentration, pH 7.5 (O. Barta, R. A. Nelson, C. Y. Kuo, Immunol. Commun. 5:75, 1976). It had a C1H50 titer of 210,000 [vs 33,000 for Cordis guinea pig (GP) C1] in a standard assay with EAC4gp, yielding a Z plot slope of 1.00.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.