Aspergillus spp. infect around 11,000,000 patients, resulting in about 600,000 deaths per year, but these numbers are on the rise due to the emergence of antifungal-resistant strains and a lack of sensitive diagnostic tests [1]. It is increasingly acknowledged that soluble pattern recognition receptors (PRRs), such as the complement component C1q, the collectins (MBL, SP, and CL-11), PTX3, and the ficolins (ficolin-1, 2, 3 and A), are important within anti-Aspergillus immunity [2]. Moreover, studies have highlighted that they may be used as a possible alternative to current antifungal drugs or used in combination to increase efficacy [3]. Binding of pathogen-associated molecular patterns (PAMPs) on the pathogen surface by soluble PRRs often results in opsonisation. This enhances interactions with membrane-associated PRRs on phagocytes, such as the important β-glucan receptor Dectin-1, Toll-like receptors (TLRs), complement receptors (CR1), and Fc receptors; ultimately augmenting phagocytosis, which is essential in controlling the infection [2]. Alternatively, opsonins can promote fungal damage directly or further promote opsonisation by C3b deposition via activation of the conserved complement system [4]. There are three main arms of the complement system, which are the classical, alternative, and lectin pathways. C1q primarily activates the classical antibody-mediated pathway, whereas MBL, CL-11, and the ficolins are known to activate the lectin complement pathway via activation of the mannose-binding lectin-associated serine proteases (MASPs). However, SP-A and SP-D are not involved in complement activation, and the role of CL-11 in Aspergillus immunity is yet to be explored. Furthermore, PTX3 can interact with complement activators and inhibitory components to modulate all three pathways [5]. The role of each of these PRRs in anti-Aspergillus immunity will be discussed further.