The majority of pathogens enter the body through mucosal surfaces and it is now evident that mucosal immunity can provide effective disease protection. However, the induction of mucosal immunity will require efficient targeting of mucosal vaccines to appropriate mucosa‐associated lymphoid tissue. An animal model, based upon the surgical preparation of sterile intestinal ‘loops’ (blind‐ended segments of intestine), was developed to evaluate mucosal and systemic immune responses to enteric vaccines in ruminants. The effectiveness of end‐to‐end intestinal anastomoses was evaluated and fetal surgery did not disrupt normal intestinal function in lambs up to 6–7 months after birth. The immunological competence of Peyer’s patches (PP) within the intestinal ‘loops’ was evaluated with a human adenovirus 5 vector expressing the gD gene of bovine herpesvirus‐1. This vaccine vector induced both mucosal and systemic immune responses when injected into intestinal ‘loops’ of 5–6‐week‐old lambs. Antibodies to the gD protein were detected in the lumen of intestinal ‘loops’ and serum and PP lymphocytes proliferated in response to gD protein. The immune competence of ileal and jejunal PP was compared and these analyses confirmed that jejunal PP are an efficient site for the induction of mucosal immune responses. This was confirmed by the presence of gD‐specific antibody‐secreting cells in jejunal but not ileal PP. Systemic but not mucosal immune responses were detected when the vaccine vector was delivered to the ileal PP. In conclusion, this model provided an effective means to evaluate the immunogenicity of potential oral vaccines and to assess the immunological competence of ileal and jejunal Peyer’s patches.

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Immune cells can acquire membrane fragments and integral membrane proteins from dead and dying cells or in the case of immature dendritic cells, from live cells. While investigating the possibility that bovine polymorphonuclear cells (PMNs) might present antigen, coculture assays confirmed that integral membrane proteins were transferred rapidly and efficiently to bovine PMNs from a variety of apoptotic and necrotic cells. Specifically, we observed that PMNs rapidly acquired proteins such as major histocompatibility complex (MHC) class II and CD3 from a variety of syngeneic, allogeneic, and xenogeneic cell types. Such acquisition occurred within 40 min of PMN coculture with isolated peripheral blood mononuclear cells, and this acquisition occurred with equal efficiency at 4 degrees C and 37 degrees C. The transfer of murine MHC class II to bovine PMNs precluded the possibility of endogenous protein expression. We also demonstrated the transfer of fluorescently labeled plasma membrane lipids and biotinylated integral membrane proteins. Collectively, these observations support the hypothesis that membrane protein transfer was mediated by the fusion of membrane fragments or microvesicles with the PMN plasma membrane and not by phagocytosis of cell fragments. These observations indicate that phenotypic studies of PMNs must consider circumstances whereby PMNs may passively acquire membrane lipids and a variety of integral membrane proteins from dead or dying cells.

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