Lagoviruses belong to the Caliciviridae family. They were first recognized as highly pathogenic viruses of the European rabbit (Oryctolagus cuniculus) and European brown hare (Lepus europaeus) that emerged in the 1970–1980s, namely, rabbit haemorrhagic disease virus (RHDV) and European brown hare syndrome virus (EBHSV), according to the host species from which they had been first detected. However, the diversity of lagoviruses has recently expanded to include new related viruses with varying pathogenicity, geographic distribution and host ranges. Together with the frequent recombination observed amongst circulating viruses, there is a clear need to establish precise guidelines for classifying and naming lagovirus strains. Therefore, here we propose a new nomenclature based on phylogenetic relationships. In this new nomenclature, a single species of lagovirus would be recognized and called Lagovirus europaeus. The species would be divided into two genogroups that correspond to RHDV- and EBHSV-related viruses, respectively. Genogroups could be subdivided into genotypes, which could themselves be subdivided into phylogenetically well-supported variants. Based on available sequences, pairwise distance cutoffs have been defined, but with the accumulation of new sequences these cutoffs may need to be revised. We propose that an international working group could coordinate the nomenclature of lagoviruses and any proposals for revision.

In contrast to adaptive antibodies, natural antibodies are present in a non-immunised organism from birth, and they do not include anti-Gal antibodies and/or anti-Gal natural antibodies, which are developed as a result of the effect of the -Gal epitope and physiological flora. Natural antibodies are the first line of the organism’s defence before the formation of the immunity created via the stimulation of elements that determine specific and non-specific immunity. This is especially important in the case of infants. Despite the fact that natural antibodies differ in their function from adaptive antibodies, they are polyreactive and they detect autoantigens and new antigenic determinants. Natural antibodies are formed from the subpopulation of B lymphocytes, mainly B1 lymphocytes and B lymphocytes of the marginal zone. This phenomenon is supported by the fact that when the quantity of these cells in the organism decreases, which happens with age, the level of natural antibodies also decreases and the risk of illnesses of old age becomes higher. During ontogenesis, these antibodies participate in many physiological processes, including the “support” of the immune system and homeostasis, the prevention of inflammation, infections and other pathological states, such as autoimmune and cardiovascular diseases, or the process of carcinogenesis. The best known natural antibody is IgM, but the role of IgGs and IgAs is also considered important. Nowadays, many researchers also mention intravenous immunoglobulins, which are used in the treatment of numerous illnesses, and there are discussions on the possibility of increasing their potential if they were based on natural antibodies.

This article reviews immunological memory cells, currently represented by T and B lymphocytes and natural killer (NK) cells, which determine a rapid and effective response against a second encounter with the same antigen. Among T lymphocytes, functions of memory cells are provided by their subsets: central memory, effector memory, tissue-resident memory, regulatory memory and stem memory T cells. Memory T and B lymphocytes have an essential role in the immunity against microbial pathogens but are also involved in autoimmunity and maternal-fetal tolerance. Furthermore, the evidence of immunological memory has been established for NK cells. NK cells can respond to haptens or viruses, which results in generation of antigen-specific memory cells. T, B and NK cells, which have a role in immunological memory, have been characterized phenotypically and functionally. During the secondary immune response, these cells are involved in the reaction against foreign antigens, including pathogens, and take part in autoimmune diseases, but also are crucial to immunological tolerance and vaccine therapy.

Melanomacrophages (MMs) are phagocytizing cells with high amounts of pigments including melanin which can be found in a number of cold-blooded species. In Osteichthyes, these cells cluster to form so-called melanomacrophage centres (MMCs), which are predominantly present in the stroma of hematopoietic and lymphoid tissues, that is, in the kidney and spleen. The functionality of MMs and MMCs results from their involvement and role in the defence reactions, related to both the innate and the adaptive immune mechanisms, and in processes unrelated to defence functions as well. There is evidence that MMCs are structurally and functionally similar to mammals’ germinal centres (GCs). It appears that mature IgM+ B cells in Osteichthyes can be the equivalent of mIgM+ centrocytes in mammals, whereas MMs can be, in terms of the function, the equivalent of follicular dendritic cells (FDCs), and MMCs can be, in terms of clustered specific cells, the equivalent of GCs. This paper presents selected facts about the structural and functional similarity between GCs and MMCs and about the involvement and role of MMCs and MMs in the immune response. The facts help get a proper picture of the location of MMs and MMCs within the structure of the fish immune system, also in the context of their evolutionary relationship with GCs and of the possibility of pointing out the evolutionary closeness between MMCs in Osteichthyes and GCs in mammals.

Butyrophilins belonging to the immunoglobulin superfamily are new immune system regulators because they are present on lymphocytes, dendritic cells, monocytes, macrophages, neutrophils and eosinophils, and they exert a stimulatory and (or) inhibitory effect on them. The role of butyrophilins is associated and results from their similarity to the regulatory B7 protein family involved in the modulation of immune phenomena. Butyrophilins are glycoproteins built of two extracellular immunoglobulin domains, stabilized with disulfide bonds: constant IgC, and variable IgV and a transmembrane region. Most of these proteins contain a conserved domain encoded by a single exon – B30.2, also referred to as PRYSPRY. In humans, the family of butyrophilins includes 7 butyrophilin proteins, 5 butyrophilin-like proteins and the SKINT-like factor. Butyrophilins have been also demonstrated to play a role in various infections, e.g. tuberculosis or diseases that include sarcoidosis, systemic lupus erythematosus, rheumatoid arthritis, genetic metabolic diseases, ulcerative colitis, cancer and kidney disease.