This analytical review of antigen-antibody interactions is intended as a guide for researchers and university teachers until the regular reaction lines of antigen-antibody interactions have been widely understood and recognized by the im-munological community. All significant relationships characterizing in vitro antigen-antibody interactions are described in detail in Section 2 and further recapitulated and listed coherently in Section 2.3. The standard formula for antigen-antibody interactions, with aggregation absent/eliminated, is . This multivariable formula shows the influence of each variable, one of which is exponential, and indicates the lines to follow to produce antibody-antigen assays of acceptable sensitivi-ty. The following false hypotheses or misleading or incomplete concepts in antigen-antibody interactions, including a spe-cial antibody-mediated condition that does not seem to have been widely recognized, were found relevant to highlight: • The equilibrium theory of virus neutralization, or virus binding, by antibodies, including the occupancy theory. These theories arose from the lack of awareness of the complexity of antigen-antibody interactions. Investigations conducted in 1978 by the author clarified the bifactorial nature of the response in conventional neu-tralization tests not influenced by complement. One reaction was the rapid, short-lasting “over-neutralization” (di-rect virus aggregation), and the second was the fundamental, monovalent, and enduring first-order reaction that documented irreversible binding between the virus and neutralizing antibodies under physiological conditions, thereby invalidating these two unsubstantiated theories. • The Percentage Law, comprising two claimed aspects: 1) the rate of neutralization is independent of the concentra-tion of the virus antigen, and 2) a percentage of the antigen is regularly resistant to neutralization. This second as-pect had led to the use of a specific term: a persistent fraction. The 1978 analyses revealed that both aspects of the Percentage Law are incorrect. The response in neutralization rate to a change in virus concentration is significant but disproportionately low. This particular low response relates to the extraordinary virus-binding capability of antibodies, but unfortunately led to the perception that the antigen's (virus) influence was insignificant. The term "neutralization rate constant" used to indicate the neutralizing potency of an antibody medium is incorrect, and a “regular persistent fraction” of the virus does not exist. Use of the term “the Percentage Law“ shall be aban-doned. However, the original observation of irregular neutralization under certain experimental conditions clearly called for further study. It is related to the formation over time of a physical barrier created by non-neutralizing antibodies under extreme experimental conditions, not to the existence of a “persistent fraction of virus”, and shall not be ex-plained by “steric hindrance”. • The theory of various weak chemical forces binding antibodies with antigens, and the related term “antibody avidi-ty”. The theory of weak binding forces, accepted in chemistry, has long been widely recognized: non-covalent interac-tions, i.e., electrostatic interactions, hydrogen bonds, van der Waals forces, and hydrophobic interactions, mediate antigen-antibody binding. However, this hypothesis 1) has never been substantiated in investigations and 2) does not explain the specificity of antigen-antibody binding. The forces binding 1) antigens with antibodies and 2) the C1q component of complement with the Fc region of sen-sitized antibodies are, therefore, so far unknown. The definition of “antibody avidity” is incorrect. (The strength of antibody binding will be related to the function of the factor q in the formula above.) • Broadly neutralizing antibodies. This expression seems to originate from a limited understanding of the regular lines of viral inactivation. In vitro, both non-neutralizing and neutralizing antibodies bind to their antigenic determinants within a specific range where they are influenced by their attractive binding force. This opens the way for two different virus-inactivating aggregation reactions: 1) the antibodies react either directly, in a synergistic action by di- or polyvalent antibodies, or 2) indirectly by interfering with the C1q aggregator of antigen-antibody complexes. Non-neutralizing antibodies are the most potent in vitro virus inactivators because of their high concentrations and rapid, aggregative inactivation of the virus. Antigen-antibody interactions in vivo shall be evaluated against regular and even irregular in vitro reactions. The term “broadly neutralizing antibodies”, not related to specified regular reactions, appears both imprecise and misleading and shall be avoided. • The secondary, inflammatory antibody-mediated, complement-activated disease complex in special tissues or organs (CADC). This item is included here because secondary disease symptoms associated with antigen-antibody interactions are not widely understood or accepted. Severe inflammatory lung disease has occurred associated with SARS-CoV-2 infection and has been described as a condition included in the acute respiratory distress syndrome, ARDS, the cause of which does not seem to have been explained when associated with infectious diseases. The secondary, antibody-mediated, complement-activated disease complex described by the author appears sud-denly, approximately 7-9 days after infection, triggered by the attainment of a threshold level of newly produced IgM and/or IgG antibodies. The background for ARDS associated with SARS-CoV-2 infection is logically ex-plained by the virus variant's pronounced lung tissue tropism and the sudden onset of the inflammatory, com-plement-activated disease. So, ample logical reasons exist to include ARDS associated with SARS-CoV-2 infec-tion into the secondary, antibody-mediated, complement-activated inflammatory disease complex. See Section 3.5 for further information on CADC. The most critical reasons for false hypotheses, misleading designations, and difficulties encountered in attempts to publish innovative research on this topic appear to be its extreme complexity, the establishment's lack of impartiality or open-mindedness, and a reluctance to accept results that diverge from widely accepted but possibly erroneous relationships. Reflective, unbiased mathematical thinking; systematically planned and performed analyses; logical deduction; and respect for science, justice, and other researchers may be the required capabilities and attitudes for researchers to promote open-mindedness and prevent future inadequate conclusions and hypotheses. Adequate lines for publishing scientific research are discussed. In vitro antigen-antibody interactions are essential for understanding both regular and irregular in vivo reactions. Investigations into the functional mechanisms of the two distinct attractive forces involved, including their potential control, are urgently needed.