The disposition of teleost memory and plasma cells (PCs) has essentially been unexplored. As the organization of the teleost immune system differs significantly from that of mammals (i.e. no bone marrow or lymph nodes, hematopoietic anterior kidney), this disposition could be essential in understanding how comparable functions are achieved. To address this question, the primary and secondary antibody-secreting cell, B memory cell, and antibody responses to T-independent and T-dependent antigens were analyzed in trout. Although the TI and TD antibody responses did not differ substantively from one another, the secondary responses to both were significantly prolonged compared with the primary responses. Logarithmic increases in titer and affinity were achieved for both antigens during the primary, with only modest increases during the secondary response. Antibody-secreting cells, both PCs and plasmablasts, quantitatively paralleled antibody production, with antibody-secreting cells skewing to the hematopoietic anterior kidney for both antigens. However, the enhanced antigen-inducible response of immune fish (indicative of the memory pool) skewed to the peripheral blood and spleen. This pattern of memory versus PC disposition parallels that observed in mammals even though the organization of the respective immune systems differs considerably. Keywords: Anterior kidney r Memory cells r Plasma cells r Trout IntroductionTeleost memory has been defined by the development of a differentially heightened responsive state to antigen, albeit lacking in a number of mammalian features. Primary immunization can, thus, lead to increased immunogen sensitivity [1], enhanced in vivo [2][3][4][5][6] and in vitro [6][7][8] antibody responsiveness, expansion of antigen-sensitive precursor pools [9] and, most importantly, anamestic responses to pathogens [4,5,10,11] and immunoprophylaxis [4,[12][13][14]. Anamestic features absent from teleost responses include isotype switching [15] (although they possess multiple isotypes [16]), relatively modest somatic mutaCorrespondence: Dr. Stephen L. Kaattari e-mail: kaattari@vims.edu tion [17][18][19] and affinity maturation [20][21][22] as compared with the IgG responses of mammals. Intriguingly, characteristics of teleost memory B cells (MBCs) [9] parallel those associated with a class of mammalian MBCs. Recent evidence reveals that human MBCs can include unswitched, mutated IgM + cells [23]; nonmutated, CD27 + IgM + cells [24], those induced by T-independent (TI) antigens [25,26], preimmune diversified repertoires [27] (as has recently been posed for the catfish [19]), or arise independently of GCs [27,28]. Together, these previous studies prompt a renewed focus on the critical elements of μ specific memory, both in teleosts and mammals. For example, perhaps the requisites for exceptionally high-titered, extensively mutated, high-affinity responses in * These authors contributed equally to this work. [32][33][34], which home to their respective hematopoietic tissues, even though the organs ...
White spot syndrome virus (WSSV) is one of the most virulent pathogens affecting penaeid shrimp, causing high mortality in infected populations. Interactions between virus structural proteins are likely to be important for virus assembly. Many steps of the WSSV assembly and maturation pathway remain unclear. In the present study, the interaction between VP37 and envelope or nucleocapsid proteins was characterized. VP37 was expressed in Escherichia coli and confirmed by Western blotting. Pure WSSV virions were subjected to Triton X-100 treatment to separate the envelope and nucleocapsid fractions. Overlay assays showed that VP37 interacted with VP28 and VP26. The interaction of VP37 with VP28 and VP26 was confirmed further by His pull-down and matrixassisted laser desorption ionization (MALDI) mass spectrographic assays. The binding assay of VP37 with VP28 by ELISA confirmed that the 2 proteins had direct interaction in vivo. This discovery will help elucidate the molecular mechanisms of virion morphogenesis. KEY WORDS: White spot syndrome virus · VP37 · Virus protein interactionResale or republication not permitted without written consent of the publisher
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