Protein or peptide, especially for prophylaxis and / or treatment of an infection and / or infectious disease and / or a sequela thereof

Abstract

The invention relates to a protein or peptide, comprising- a first protein portion or peptide portion, a second protein portion or peptide portion and a third protein portion or peptide portion, wherein - in direction of the C terminus of the protein or peptide, the second protein portion or peptide portion is located after the first protein portion or peptide portion, and the third protein portion or peptide portion is located after the second protein portion or peptide portion, - the first protein portion or peptide portion has an amino acid sequence or consists of an amino acid sequence that corresponds to a partial sequence of a surfactant protein or to a variant of a partial sequence of a surfactant protein, - the third protein portion or peptide portion has an amino acid sequence or consists of an amino acid sequence that corresponds to a different partial sequence of the surfactant protein or to a variant of a different partial sequence of the surfactant protein or to a partial sequence of a different surfactant protein or to a variant of a partial sequence of a different surfactant protein, and - the second protein portion or peptide portion has an amino acid sequence or consists of an amino acid sequence that corresponds to a complete amino acid sequence or to a partial sequence of ACE2 or to a variant of a complete amino acid sequence or to a variant of a partial sequence of ACE2. The invention further relates to a nucleic acid, to an expression vector, to a host cell, to a conjugate and to a pharmaceutical composition.

Description

[0001] Protein or peptide, in particular for the prophylaxis and / or treatment of an infection and / or infectious disease and / or a secondary disease thereof FIELD OF APPLICATION AND PRIOR ART The invention relates to a protein or peptide, a nucleic acid, an expression vector, a host cell, a conjugate and a pharmaceutical composition, in particular for use in the prophylaxis and / or treatment of an infection and / or infectious disease, in particular respiratory disease, caused by viruses, in particular coronaviruses, preferably SARS-CoV-2, and / or a secondary disease thereof. Coronaviruses, also known as Coronaviridae, are enveloped single-stranded viruses. The 120 nm to 160 nm large virus particles (virions) have a virus envelope into which several different membrane proteins are embedded.The characteristic appearance of coronaviruses is due to the numerous club-shaped structures on their surface, called spikes, which protrude approximately 20 nm outward. They consist of the S1 and S2 subunits. The S1 subunit carries the receptor-binding domain (RBD), which enables the virus to dock onto a cell. The S2 subunit causes the fusion of the viral envelope and cell membrane, thus internalizing the virus particles into a cell (the so-called host cell). The smaller envelope protein (E protein, 9 to 12 kDa) is present in small amounts on the outer surface. Only HCoV-OC43 (Human Coronavirus OC43) and the Group 2 coronaviruses (genus Betacoronavirus) additionally contain the hemagglutin esterase protein (HE protein, 65 kDa). The M protein (matrix protein, 23 to 35 kDa), which is also anchored in the membrane envelope, is directed inwards and represents a matrix protein on the inside of the virus envelope.Inside the envelope is a presumably icosahedral capsid containing a helical nucleoprotein complex. This consists of the nucleoprotein N (50 to 60 kDa) complexed with a single-stranded RNA of positive polarity. Certain amino acid residues of the N protein interact with the matrix protein M, so that the capsid is associated with the inner surface of the membrane. The single-stranded RNA genome of coronaviruses is approximately 26,000 to 32,000 nucleotides (nt) long, making coronaviruses the longest genomes of all known RNA viruses. Coronaviruses cause very different diseases in various vertebrates such as mammals, birds, and fish. In humans, for example, coronaviruses 229E, HKU1, OC43, and NL63 cause between 10% and 30% of upper respiratory tract infections, although the illnesses are generally mild.However, there have also been severe cases in the past. For example, in 2002, 8,096 people in southern China were infected with SARS-CoV, of whom 774 died, corresponding to a mortality rate of 9.6%. In 2012, 2,494 people in 28 different countries were confirmed to have been infected with MERS-CoV, of whom 858 died, corresponding to a mortality rate of 34.4%. At the end of December 2019, a new coronavirus was identified, which the World Health Organization (WHO) has since named SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2). SARS-CoV-2 causes a respiratory disease, specifically lung disease, known as COVID-19. The viral disease was first described in Wuhan at the end of 2019. In January 2020, the viral disease developed into an epidemic in the People's Republic of China and eventually spread worldwide into the COVID-19 pandemic.The viral disease spreads primarily through droplet infection. The course of the disease is nonspecific, diverse, and varies greatly. In addition to asymptomatic infections, predominantly mild to moderate courses are observed, but severe cases with bilateral pneumonia, including respiratory failure and death, have also been observed. In addition to lung damage, pathological processes of the liver, central nervous system, and heart have also been observed. Older people and those with pre-existing conditions such as diabetes and / or high blood pressure are particularly at increased risk of developing COVID-19. To penetrate a host cell, the SARS-CoV-2 spikes interact with the transmembrane receptor ACE2 (angiotensin-converting enzyme 2). ACE2 is present not only in human tissues but also in other mammals.While the S1 subunit of SARS-CoV-2 forms the receptor-binding domain (RBD) for binding to the ACE2 receptor, the S2 subunit, consisting of a fusion peptide (FP), hepatrepeat 1 (HR1), hepatrepeat 2 (HR2), a transmembrane domain (TM), and a cytoplasmic fusion domain (CP), is responsible for viral cell fusion and cell entry into type II alveolar epithelial cells (type II pneumocytes) of the alveoli. During the viral infection process, endogenous proteases activate the spike protein S by cleaving it into its two subunits S1 and S2. In the case of SARS-CoV-2, these proteases are transmembrane serine protease 2 and respiratory trypsin-like protease (HAT). Viral endocytosis depends on cathepsin L (CPL), a pH-dependent cysteine ​​protease found in endosomes. Vesicle pinching depends on dynamin.Intensive research is currently being conducted into active substances for the prevention and / or treatment of COVID-19. Both established drugs, such as the malaria drug hydroxychloroquine and the Ebola drug remdesivir, as well as newly developed active substances are being tested for their therapeutic efficacy against SARS-CoV-2. On January 28, 2022, the combination of the protease inhibitor nirmatrelvir and ritonavir was approved in the EU and subsequently used for the treatment of COVID under the trade name Paxlovid®. A therapeutic breakthrough is currently pending. In addition, a number of vaccines against SARS-COVID-19 have been developed, including protein-based vaccines, mRNA-based vaccines, DNA-based vaccines, vaccines with vector viruses, vaccines with inactivated SARS-CoV-2, and vaccines with attenuated SARS-CoV-2.Despite good acceptance of such vaccinations among the global population, the course of disease following a SARC-CoV-2 infection has improved, but a still high number of SARS-CoV-2 infections and the associated COVID-19 disease have not been contained. Thus, vaccine breakthroughs still frequently occur, in which people become infected with SARS-CoV-2 and become ill despite being fully vaccinated. The fact that existing vaccinations do not provide complete protection against SARS-CoV-2 infection may be due, among other things, to the fact that the infection occurs via the air, but the blood-air barrier, which in the lungs separates the air-filled space of the alveoli from the blood in the capillaries, does not allow a sufficient number of antibodies from the bloodstream to pass through to the surface of the alveoli. The blood-air barrier consists of a layer consisting of type I pneumocytes, the capillary endothelium, and the normally fused basal lamina located between them.Previously known antiviral drugs for the treatment of SARS-CoV-2 infection often pursue the approach of blocking viral replication intracellularly, strengthening the immune system, or alleviating symptoms, particularly those related to the cardiovascular system. An alternative approach is antiviral drugs that prevent SARS-CoV-2 from entering cells. Such antiviral drugs are, for example, modeled on antibodies or involve mRNA-based vaccines that are delivered directly to the lungs through inhalation. Another approach is to prevent the binding between SARS-CoV-2 and ACE2 using proteins or peptides, for example, by inhibiting the formation of the serine protease TMPRSS2, which is involved in the binding of SARS-CoV-2 and ACE.However, disadvantages of previously known antiviral agents in the form of proteins or peptides that disrupt the binding between SARS-CoV-2 and ACE are that their production, especially cellular production, is difficult, and the proteins or peptides produced in this way are often unstable and therefore unsuitable as antiviral agents. Accordingly, there remains a great need for alternative antiviral agents for the prevention and / or treatment of infections and / or infectious diseases, especially infections and / or infectious diseases caused by coronaviruses, especially SARS-CoV-2, and / or any resulting complications.TASK AND SOLUTION It is therefore an object of the invention to provide an active ingredient which is particularly suitable for the prevention and / or treatment of infections and / or infectious diseases, in particular infections and / or infectious diseases caused by coronaviruses, in particular SARS-CoV-2, and / or secondary diseases thereof. Furthermore, it is an object of the invention to provide a nucleic acid encoding the protein or peptide, an expression vector, a host cell, a conjugate and a pharmaceutical composition. These objects are achieved by a protein or peptide according to independent claim 1, a nucleic acid according to claim 23, an expression vector according to claim 23, a host cell according to claim 23, a conjugate according to claim 24 and by a pharmaceutical composition according to claim 25. Preferred embodiments of the invention are the subject of the dependent claims and the general description.The wording of all claims is hereby incorporated by express reference into the content of the description. According to a first aspect, the invention relates to a protein or peptide, in particular a polypeptide. The protein or peptide can be a chemically produced protein, i.e. a protein or peptide produced by chemical synthesis and / or laboratory techniques, or a recombinant protein or peptide, i.e. a protein or peptide produced biotechnologically and / or molecularly, in particular a chimeric protein or peptide or fusion protein or fusion peptide. The protein or peptide has a first protein or peptide section, a second protein or peptide section and a third protein or peptide section.Starting from the N-terminus towards the C-terminus of the protein or peptide, the second protein or peptide segment is arranged behind the first protein or peptide segment, in particular directly or not directly. The third protein or peptide segment is arranged from the N-terminus towards the C-terminus of the protein or peptide behind the second protein or peptide segment, in particular directly or not directly. The first protein or peptide segment has an amino acid sequence that corresponds to a partial sequence of a surfactant protein or to a variant of a partial sequence of a surfactant protein. Alternatively, the first protein or peptide segment consists of an amino acid sequence that corresponds to a partial sequence of a surfactant protein or to a variant of a partial sequence of a surfactant protein.The third protein or peptide section has an amino acid sequence that corresponds to a different partial sequence of the surfactant protein or to a variant of a different partial sequence of the surfactant protein. Alternatively, the third protein or peptide section consists of an amino acid sequence that corresponds to a different partial sequence of the surfactant protein or to a variant of a different partial sequence of the surfactant protein. Alternatively, the third protein or peptide section consists of an amino acid sequence that corresponds to a partial sequence of a different surfactant protein or to a variant of a partial sequence of a different surfactant protein. Alternatively, the third protein or peptide section consists of an amino acid sequence that corresponds to a partial sequence of a different surfactant protein or to a variant of a partial sequence of a different surfactant protein.The second protein or peptide portion has an amino acid sequence that corresponds to a complete amino acid sequence of ACE2 (angiotensin-converting enzyme 2). Alternatively, the second protein or peptide portion has an amino acid sequence that corresponds to a variant of a complete amino acid sequence of ACE2. Alternatively, the second protein or peptide portion has an amino acid sequence that corresponds to a partial sequence of ACE2. Alternatively, the second protein or peptide portion has an amino acid sequence that corresponds to a variant of a partial sequence of ACE2. Alternatively, the second protein or peptide portion consists of an amino acid sequence that corresponds to a complete amino acid sequence of ACE2. Alternatively, the second protein or peptide portion consists of an amino acid sequence that corresponds to a variant of a complete amino acid sequence of ACE2.Alternatively, the second protein or peptide section consists of an amino acid sequence which corresponds to a partial sequence of ACE2. Alternatively, the second protein or peptide section consists of an amino acid sequence which corresponds to a variant of a partial sequence of ACE2. Preferably, the above-mentioned ACE2, i.e. the ACE2 of the present invention, is a human ACE2. Alternatively, the ACE2 of the present invention can be a non-human ACE2. Further preferably, the above-mentioned surfactant protein and / or the above-mentioned other surfactant protein, in particular in each case, is a human surfactant protein. Alternatively, the above-mentioned surfactant protein and / or the above-mentioned other surfactant protein, in particular in each case, can be a non-human surfactant protein.The term "partial sequence" in the sense of the present invention is to be understood as a partial sequence of an amino acid sequence. The term "surfactant" in the sense of the present invention is to be understood as a surface-active composition produced by type II alveolar epithelial cells (type II pneumocytes) in the lungs and secreted onto the surface of the alveolar epithelium. The largest proportion of the composition is made up of lipids. In addition, the composition comprises proteins, among others surfactant proteins, in particular the aforementioned proteins surfactant protein A and surfactant protein D. The term "variant" of a respective amino acid sequence in the sense of the present invention is to be understood as meaning in particular an insertion and / or addition and / or deletion and / or substitution variant of the respective amino acid sequence, iean amino acid sequence that differs from the respective amino acid sequence by one or more insertions and / or by one or more additions and / or by one or more deletions and / or by one or more substitutions of amino acids or amino acid residues. The variant can therefore in particular be a partial sequence of the respective amino acid sequence. Preferably, the variant has a sequence identity or sequence homology to the respective amino acid sequence of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. For the purposes of the present invention, the term “sequence identity” between two amino acid sequences is understood to mean the percentage or proportion of amino acids or amino acid residues that are identical between the amino acid sequences.The invention is characterized in particular by the following advantages: - The amino acid sequence of the second protein or peptide segment particularly advantageously contains the binding motif or sequence for SARS-CoV-2. As a result, the protein or peptide is capable of competitively antagonizing the virus, reducing or even completely preventing binding of the virus to its host cells, in particular to human alveolar epithelial cells of type II, and thus internalization of the virus into its host cells, in particular into human alveolar epithelial cells of type II. This advantageously enables prophylaxis and / or treatment, in particular symptomatic treatment, in particular of infections and / or infectious diseases and / or sequelae caused by SARS-CoV-2.Compared to artificially produced antibodies, binding-affinity nanobodies, or some active vaccines that trigger a natural antibody response in the vaccinated person to a limited number of viral surface properties, ACE2 binding motifs have the advantage that, as archaic endogenous constructs, they are also suitable for potential SARS-CoV-2 mutants, provided they are clinically pathogenic—because this pathogenicity necessarily requires cell intrusion via ACE2 at the surfaces of alveolar epithelial cells. This binding of viruses to endogenous ACE2 can, in turn, be disrupted or inhibited by mobile ACE2 motifs, which are available in abundance, as part of a competition, or viruses can be bound to mobile constructs and intercepted for further beneficial immunological processes, thus neutralizing them.- The use of a complete ACE2 molecule or an ACE2 dimer, as described, for example, in EP 2543724 A2, is advantageously unnecessary. - The surfactant protein amino acid sequences of the first and third protein or peptide segments enable macrophages, in particular alveolar macrophages, to approximate SARS-CoV-2 virus particles bound to the second protein or peptide segment of the protein or peptide according to the invention. This particularly advantageously achieves immunogenic virus neutralization. - A further advantage is that the protein or peptide according to the invention can reduce or even completely prevent active agonization of the transmembrane ACE2 receptor due to virus saturation, which occurs through binding of the protein or peptide according to the invention to SARS-CoV-2.This can also reduce or even completely eliminate the risk of widespread damage, such as blood vessel damage, and associated pathogenic processes such as blood clotting disorders arising from the activation of subsequent signal transduction cascades. As mentioned above, virus neutralization, particularly specific virus neutralization, can be achieved with the protein or peptide. A treatment based on this approach has the advantage over virucidal treatment in that it has significantly fewer or almost no side effects.Because, in particular, virus killing does not occur, but rather the active viral surface is predominantly covered by binding to the protein or peptide, which in turn inhibits or prevents viral cell invasion, the patient's body is able to develop antibodies against the virus and thus corresponding immunity despite attenuated viral disease activity. - A further advantage is that the amino acid sequence of the first and / or third protein or peptide segment can generally create an affinity between the protein or peptide according to the invention and a patient's surfactant. This can be used to particularly advantageously counteract the collapse of a patient's alveoli. - The protective effect of conventional vaccinations against SARS-CoV-2 has so far been exerted primarily by antibodies produced by vaccination.However, SARS-CoV-2 infection does not occur in the bloodstream, where most antibodies are located, but in the lungs, where few vaccine-induced antibodies are present. The protein or peptide according to the invention advantageously enables treatment mechanisms, particularly in combination with a conventional vaccination, that act directly at the site of SARS-CoV-2 infection by allowing the protein or peptide to enter the lungs, particularly through inhalation. Preferably, the protein or peptide is free of an amino acid sequence that corresponds to the amino acid sequence of the cytoplasmic chain of ACE2. This advantageously prevents the initiation of undesirable so-called second messenger processes in host cells, particularly in type II alveolar epithelial cells.More preferably, the protein or peptide is free of an amino acid sequence that corresponds to the amino acid sequence of the transmembrane domain of ACE2 or a variant, in particular a partial sequence, thereof. This can particularly advantageously prevent integration of the protein or peptide into a membrane of host cells, in particular type II alveolar epithelial cells, and thus an increase in the cellular binding surface for the virus and thus an augmentation of infection. In an embodiment of the invention, the partial sequence of the surfactant protein is a partial sequence that begins at the N-terminus of the surfactant protein, and the other partial sequence of the surfactant protein, or the partial sequence of the other surfactant protein, is a partial sequence that ends at the C-terminus of the surfactant protein or the other surfactant protein.In a further embodiment of the invention, the partial sequence and / or other partial sequence of the surfactant protein is a complete amino acid sequence or a partial sequence of a subunit of the surfactant protein, or a variant of a complete amino acid sequence or a partial sequence of a subunit of the surfactant protein. In a further embodiment of the invention, the partial sequence of the other surfactant protein is a complete amino acid sequence or a partial sequence of a subunit of the other surfactant protein, or a variant of a complete amino acid sequence or a partial sequence of a subunit of the other surfactant protein.In a further embodiment of the invention, the amino acid sequence of the first protein or peptide section and the amino acid sequence of the third protein or peptide section together correspond to a complete amino acid sequence of the surfactant protein or a variant of a complete amino acid sequence of the surfactant protein. In a further embodiment of the invention, the surfactant protein is selected from the group consisting of surfactant protein A, surfactant protein B, surfactant protein C, surfactant protein D and a combination of at least two of the aforementioned surfactant proteins. Preferably, the surfactant protein is surfactant protein A or surfactant protein D. In a further embodiment of the invention, the other surfactant protein is selected from the group consisting of surfactant protein A, surfactant protein B, surfactant protein C, surfactant protein D and a combination of at least two of the aforementioned surfactant proteins.The other surfactant protein is preferably surfactant protein A or surfactant protein D. In a further embodiment of the invention, the surfactant protein is surfactant protein D. As a result, the protein or peptide according to the invention is advantageously also capable of effecting immunogenic virus neutralization via the approximation of macrophages, in particular alveolar macrophages, to SARS-CoV-2 virus particles bound to the second protein or peptide segment of the protein or peptide according to the invention. In this case, a further advantage is that the amino acid sequence of the surfactant protein and / or the other surfactant protein creates an additional binding site for SARS-CoV-2 virus particles.As a result, virus saturation by the protein or peptide according to the invention can be further optimized and the risk of virus particles, in particular of SARS-CoV-2, infecting host cells, in particular type II alveolar epithelial cells, can be further reduced or even completely avoided. Furthermore, this advantageously supports the phagocytosis of bound virus particles. In a further embodiment of the invention, the surfactant protein is surfactant protein D and the other surfactant protein is surfactant protein A. This allows the positive effects described in the previous paragraph to be advantageously combined. In a further embodiment of the invention, the surfactant protein is surfactant protein A and the other surfactant protein is surfactant protein D. This allows the positive effects described in the penultimate paragraph to be advantageously combined.In a further embodiment of the invention, the amino acid sequence of the first protein or peptide section and / or the amino acid sequence of the third protein or peptide section comprise / comprises a partial sequence of an amino acid sequence according to sequence ID number: 1 (entire surfactant protein D) or a variant of an amino acid sequence according to sequence ID number: 1 (entire surfactant protein D), or the amino acid sequence of the first protein or peptide section and / or the amino acid sequence of the third protein or peptide section consists / comprises a partial sequence of an amino acid sequence according to sequence ID number: 1 (entire surfactant protein D) or a variant of an amino acid sequence according to sequence ID number: 1 (entire surfactant protein D). The amino acid sequence according to sequence ID number: 1 corresponds to the amino acid sequence of surfactant protein D.The sequence ID number: 1 preferably consists of a signal sequence (amino acid residues from position 1 to 21), an N-terminal domain (amino acid residues from position 22 to 45), a collagen-like repeat domain, in particular necessary for the dodecamerization of the protein or peptide (amino acid residues from position 46 to 222), a coiled-coil neck domain, in particular necessary for the trimerization of the protein or peptide (amino acid residues from position 223 to 259), and a C-type lectin domain (amino acid residues from position 260 to 375). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 1 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%.In a further embodiment of the invention, the amino acid sequence of the first protein or peptide section has an amino acid sequence glycine, leucine, lysine (Gly, Leu, Lys), in particular starting from the N-terminus towards the C-terminus of the protein or peptide, which preferably corresponds to the amino acid sequence at positions 202 to 204 of surfactant protein D (sequence ID number: 1), or a variant thereof, or the amino acid sequence of the first protein or peptide section consists of an amino acid sequence glycine, leucine, lysine (Gly, Leu, Lys), in particular starting from the N-terminus towards the C-terminus of the protein or peptide, which preferably corresponds to the amino acid sequence at positions 202 to 204 of surfactant protein D (sequence ID number: 1), or a variant thereof. The amino acid residues mentioned in the previous paragraph form a collagen-like repeat sequence.The retention of these amino acid residues and thus the retention of the collagen-like repeat sequence is particularly advantageous for the stability, in particular for the dodecamerization, of the protein or peptide according to the invention, in particular the amino acid sequence of the surfactant protein D. Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence glycine, leucine, lysine (Gly, Leu, Lys) of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%.In a further embodiment of the invention, the amino acid sequence of the first protein or peptide segment has an amino acid sequence according to sequence ID number: 2 (Gly205-Pro222 of surfactant protein D) or a variant thereof, or the amino acid sequence of the first protein or peptide segment consists of an amino acid sequence according to sequence ID number: 2 (Gly205-Pro222 of surfactant protein D) or a variant thereof. The amino acid sequence according to sequence ID number: 2 corresponds to amino acid residues 205 to 222 of surfactant protein D and partially contains a coiled-coil neck domain. Preserving this domain is particularly advantageous for the stability of the quaternary structure, in particular trimerization, of the protein or peptide according to the invention, in particular the amino acid sequence of surfactant protein D.Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 2 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the amino acid sequence of the first protein or peptide segment comprises an amino acid sequence according to sequence ID number: 3 (Met1-Pro222 of surfactant protein D) or a variant thereof, or the amino acid sequence of the first protein or peptide segment consists of an amino acid sequence according to sequence ID number: 3 (Met1-Pro222 of surfactant protein D) or a variant thereof. The amino acid sequence according to sequence ID number: 3 corresponds to amino acid residues 1 to 222 of surfactant protein D. Preferably, sequence ID number: 3 comprises a signal sequence (amino acid residues from positions 1 to 21).Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 3 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the amino acid sequence of the third protein or peptide segment comprises an amino acid sequence according to sequence ID number: 4 (Asp 223 to Phe 375 of surfactant protein D) or a variant thereof, or the amino acid sequence of the third protein or peptide segment consists of an amino acid sequence according to sequence ID number: 4 (Asp 223 to Phe 375 of surfactant protein D) or a variant thereof. The amino acid sequence according to sequence ID number: 4 corresponds to amino acid residues 223 to 375 of surfactant protein D.Preferably, the sequence ID number 4 consists of a coiled-coil neck domain, in particular necessary for the trimerization of the protein or peptide (amino acid residues from positions 1 to 37), and a C-type lectin domain (amino acid residues from positions 38 to 153). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number 4 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the complete amino acid sequence or the partial sequence of ACE2 comprises the lysine located at position 31 of ACE2, the glutamate located at position 35 of ACE2, the aspartate located at position 38 of ACE2 and the methionine located at position 82 of ACE2.Retaining these positions is particularly advantageous for binding of SARS-CoV-2 to the protein or peptide of the invention. In a further embodiment of the invention, the partial sequence of ACE2 is a complete amino acid sequence or a partial sequence of an ectopic domain of ACE2, or a variant of a complete amino acid sequence or a partial sequence of an ectopic domain of ACE2.In a further embodiment of the invention, the amino acid sequence of the second protein or peptide section comprises a partial sequence of an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2) or a variant of a partial sequence of an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2), or the amino acid sequence of the second protein or peptide section consists of a partial sequence of an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2) or a variant of a partial sequence of an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2). The amino acid sequence according to sequence ID number: 5 corresponds to the complete amino acid sequence of ACE2. Preferably, sequence ID number: 5 comprises a signal sequence (amino acid residues from positions 1 to 21).Preferably, the variant has a sequence identity or sequence homology of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% to the partial sequence of the amino acid sequence according to sequence ID number: 5. In a further embodiment of the invention, the partial sequence of the amino acid sequence according to sequence ID number 5 is selected from the group consisting of sequence ID number 6 (Ser19-Asn90 of ACE2), sequence ID number 7 (I-363 of ACE2), sequence ID number 8 (I-467 of ACE2), sequence ID number 9 (I-563 of ACE2), and sequence ID number 10 (complete amino acid sequence of the ectopic domain of ACE2). The amino acid sequence according to sequence ID number 6 corresponds to amino acid residues 19 to 90 of ACE2 and contains a binding site for SARS-CoV2. Preserving this sequence is particularly advantageous for the binding between SAS-CoV2 and the protein or peptide according to the invention.Within sequence ID number 6, the amino acid residues lysine (K, position 31), glutamine (E, position 35), asparagine (D, position 38), and methionine (M, position 82) are particularly advantageous for binding between SARS-CoV2 and the protein or peptide according to the invention. Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number 6 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. Furthermore, the amino acid sequence according to sequence ID number 6 forms the first two alpha helices of surfactant protein D. For this reason, the amino acid sequence according to sequence ID number 6 is particularly advantageous for the binding between SAS-CoV2 and the protein or peptide of the invention. The amino acid sequence according to sequence ID number 7 corresponds to amino acid residues 1 to 363 of ACE2.Preferably, Sequence ID number 7 has a signal sequence (amino acid residues from positions 1 to 21). Preferably, the variant has a sequence identity or sequence homology of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% to the amino acid sequence according to Sequence ID number 7. The amino acid sequence according to Sequence ID number 8 corresponds to amino acid residues 1 to 467 of ACE2. Preferably, Sequence ID number: 8 has a signal sequence (amino acid residues from positions 1 to 21). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to Sequence ID number: 8 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%.The amino acid sequence according to sequence ID number: 9 corresponds to amino acid residues 1 to 563 of ACE2. Preferably, sequence ID number: 9 has a signal sequence (amino acid residues from positions 1 to 21). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 9 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. The amino acid sequence according to sequence ID number 10 corresponds to the complete amino acid sequence of the ectopic domain of ACE2. Preferably, sequence ID number 10 contains a signal sequence (amino acid residues from positions 1 to 21).Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 10 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the amino acid sequence of the second protein or peptide section has an amino acid sequence according to sequence ID number: 6 (Ser19-Asn90 of ACE2) or a variant of an amino acid sequence according to sequence ID number: 6 (Ser19-Asn90 of ACE2) or the amino acid sequence of the second protein or peptide section consists of an amino acid sequence according to sequence ID number: 6 (Ser19-Asn90 of ACE2) or a variant of an amino acid sequence according to sequence ID number: 6 (Ser19-Asn90 of ACE2).In a further embodiment of the invention, the amino acid sequence of the second protein or peptide section has an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2) or a variant thereof, or the amino acid sequence of the second protein or peptide section consists of an amino acid sequence according to sequence ID number: 5 (complete amino acid sequence of ACE2) or a variant thereof. Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 5 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the N-terminus of the protein or peptide is the N-terminus of the first protein or peptide segment.This advantageously improves the stability of the protein or peptide, in particular its secondary and tertiary structure. In a further embodiment of the invention, the C-terminus of the protein or peptide is the C-terminus of the third protein or peptide segment. This also advantageously improves the stability of the protein or peptide, in particular its secondary and tertiary structure. In a further embodiment of the invention, the protein or peptide has an amino acid sequence according to sequence ID number: 11 or a variant thereof, or the protein or peptide consists of an amino acid sequence according to sequence ID number: 11 or a variant thereof. The amino acid sequence according to sequence ID number: 11 corresponds to amino acid residues 1 to 222 of surfactant protein D, amino acid residues 19 to 90 of ACE2, and amino acid residues 223 to 375 of surfactant protein D.The sequence ID number: 11 preferably consists of the signal sequence of surfactant protein D (amino acid residues from position 1 to 21), the N-terminal domain of surfactant protein D (amino acid residues from position 22 to 45), the collagen-like repeat domain of surfactant protein D, in particular necessary for the dodecamerization of the protein or peptide (amino acid residues from position 46 to 222), the amino acid residues 19 to 90 of ACE2 (amino acid residues from position 223 to 294), the coiled-coil neck domain of surfactant protein D, in particular necessary for the trimerization of the protein or peptide (amino acid residues from position 295 to 331), and the C-type lectin domain of surfactant protein D (amino acid residues from position 332 to 447).Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 11 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%.Furthermore, the amino acid sequence of the second protein or peptide section can comprise a partial sequence of an amino acid sequence according to sequence ID number: 12 (complete amino acid sequence of ACE2 with Gly at position two of the amino acid sequence) or a variant of a partial sequence of an amino acid sequence according to sequence ID number: 12 (complete amino acid sequence of ACE2 with Gly at position two of the amino acid sequence) or consist of a partial sequence of an amino acid sequence according to sequence ID number: 12 (complete amino acid sequence of ACE2 with Gly at position two of the amino acid sequence) or a variant of a partial sequence of an amino acid sequence according to sequence ID number: 12 (complete amino acid sequence of ACE2 with Gly at position two of the amino acid sequence). The amino acid sequence according to sequence ID number: 12 corresponds to the complete amino acid sequence of ACE2 with glycine (Gly, G) at position two of the amino acid sequence.Preferably, sequence ID number 12 has a signal sequence (amino acid residues from positions 1 to 22). Preferably, the variant has a sequence identity or sequence homology to the partial sequence of the amino acid sequence according to sequence ID number 12 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. Preferably, the partial sequence of the amino acid sequence according to sequence ID number: 12 is selected from the group consisting of sequence ID number: 6 (Ser19-Asn90 of ACE2), sequence ID number: 13 (I-364 of ACE2 with Gly at position two of the amino acid sequence), sequence ID number: 14 (I-468 of ACE2 with Gly at position two of the amino acid sequence), sequence ID number: 15 (I-564 of ACE2 with Gly at position two of the amino acid sequence) and sequence ID number: 16 (complete amino acid sequence of the ectopic domain of ACE2 with Gly at position two of the amino acid sequence).The amino acid sequence according to sequence ID number: 13 corresponds to amino acid residues 1 to 364 of ACE2 with glycine (Gly, G) at position two of the amino acid sequence. Preferably, sequence ID number: 13 has a signal sequence (amino acid residues from positions 1 to 22). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 13 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. The amino acid sequence according to sequence ID number 14 corresponds to amino acid residues 1 to 468 of ACE2 with glycine (Gly, G) at position two of the amino acid sequence. Preferably, sequence ID number 14 contains a signal sequence (amino acid residues from positions 1 to 22).Preferably, the variant has a sequence identity or sequence homology of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% to the amino acid sequence according to sequence ID number 14. The amino acid sequence according to sequence ID number 15 corresponds to amino acid residues 1 to 564 of ACE2 with glycine (Gly, G) at position two of the amino acid sequence. Preferably, sequence ID number 15 has a signal sequence (amino acid residues from positions 1 to 22). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 15 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%.The amino acid sequence according to sequence ID number: 16 corresponds to the complete amino acid sequence of the ectopic domain of ACE2 with glycine (Gly, G) at position two of the amino acid sequence. Preferably, sequence ID number: 16 has a signal sequence (amino acid residues from positions 1 to 22). Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 16 of, in particular, at least 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99%. In a further embodiment of the invention, the protein or peptide is a protein or peptide for use in prophylaxis, iePrevention and / or treatment of an infection and / or infectious disease caused by viruses, preferably by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof. In particular, the protein or peptide can be a protein or peptide for use in vaccination against an infection and / or infectious disease caused by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof. The infectious disease, in particular a respiratory disease, can be an acute or chronic respiratory disease.Preferably, the infectious disease, in particular a respiratory disease, is selected from the group consisting of pneumonia, acute bronchitis, colds, influenza, tonsillitis, laryngitis, sinusitis, bronchial asthma, chronic bronchitis, and chronic obstructive pulmonary disease (COPD). Preferably, the infectious disease, in particular a respiratory disease, is pneumonia. Particularly preferably, the infectious disease, in particular a respiratory disease, is viral pneumonia, i.e., a viral pneumonia, i.e., a pneumonia caused by viruses. Most preferably, the infectious disease, in particular a respiratory disease, is COVID-19, i.e., a respiratory disease, in particular pneumonia, caused by SARS-CoV-2.The secondary disease is preferably selected from the group consisting of idiopathic pulmonary hypertension, acute organ failure such as acute lung failure (ARDS, Acute Respiratory Distress Syndrome) or acute kidney failure, pulmonary fibrosis, thrombosis, thromboembolism, blood vessel damage, blood clotting disorders and inflammatory diseases such as PIMS (Paediatric Inflammatory Multisystem Syndrome) or Kawasaki syndrome. Furthermore, the protein or peptide may further comprise a linker unit. The linker unit may be arranged or formed in particular in the direction of the C-terminus of the protein or peptide behind, in particular directly or not directly behind, the first, second or third protein or peptide section. The linker unit may in particular be a peptide linker unit, i.e. a linker unit comprising peptide bonds. The linker unit may comprise a number of cysteine ​​residues, i.e.one cysteine ​​residue or more cysteine ​​residues, in particular 1 cysteine ​​residue to 5 cysteine ​​residues, or consist of a number of cysteine ​​residues, i.e. one cysteine ​​residue or more cysteine ​​residues, in particular 1 cysteine ​​residue to 5 cysteine ​​residues. Alternatively or in combination, the linker unit can have a number of glutathione residues, i.e. one glutathione residue or more glutathione residues, or consist of a number of glutathione residues, i.e. one glutathione residue or more glutathione residues. Alternatively or in combination, the linker unit can have glutathione S-transferase or consist of glutathione S-transferase. Alternatively or in combination, the linker unit can have a number of penicillamine residues, i.e. one penicillamine residue or more penicillamine residues, or consist of a number of penicillamine residues, i.e. one penicillamine residue or more penicillamine residues.Alternatively or in combination, the linker unit can comprise the peptide SpyTag or consist of the peptide SpyTag. Alternatively or in combination, the linker unit can comprise the protein SpyCatcher or consist of the protein SpyCatcher. Preferably, the linker unit has an amino acid sequence according to sequence ID number: 17 or preferably the linker unit consists of an amino acid sequence according to sequence ID number: 17 (5 cysteine ​​residues). Alternatively, preferably, the linker unit has an amino acid sequence according to sequence ID number: 17 or a variant thereof, or alternatively, preferably the linker unit consists of an amino acid sequence according to sequence ID number: 17 or a variant thereof. The amino acid sequence according to sequence ID number: 18 corresponds to the amino acid sequence of glutathione S-transferase.Preferably, the variant has a sequence identity or sequence homology of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% to the amino acid sequence according to sequence ID number: 17 and / or according to sequence ID number: 18. According to a second aspect, the invention relates to a nucleic acid, in particular a DNA sequence or RNA sequence, in particular an mRNA sequence. The nucleic acid, in particular a DNA sequence or RNA sequence, in particular an mRNA sequence, encodes a protein or peptide according to the first aspect of the invention. Preferably, the nucleic acid, in particular DNA sequence or RNA sequence, in particular mRNA sequence, codes for an amino acid sequence according to sequence ID number: 11 or a variant thereof.Preferably, the variant has a sequence identity or sequence homology of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% to the amino acid sequence according to sequence ID number: 11. In particular, the nucleic acid can be a nucleic acid for use in the prophylaxis, i.e. prevention, and / or treatment of an infection and / or infectious disease caused by viruses, preferably by coronaviruses, particularly preferably by SARS-CoV-2, and / or by bacteria, in particular respiratory disease, and / or a secondary disease thereof.In particular, the nucleic acid can be a nucleic acid for use in vaccination against an infection and / or infectious disease caused by coronaviruses, particularly preferably by SARS-CoV-2, and / or an infection and / or infectious disease, in particular a respiratory disease, and / or a secondary disease thereof, caused by bacteria. The infectious disease, in particular a respiratory disease, can be an acute or chronic respiratory disease. Preferably, the infectious disease, in particular a respiratory disease, is selected from the group consisting of pneumonia, acute bronchitis, the common cold, influenza, tonsillitis, laryngitis, sinusitis, bronchial asthma, chronic bronchitis, and chronic obstructive pulmonary disease (COPD). The infectious disease, in particular a respiratory disease, is preferably pneumonia.Particularly preferably, the infectious disease, in particular a respiratory disease, is viral pneumonia, i.e., a viral pneumonia, i.e., a pneumonia caused by viruses. Most preferably, the infectious disease, in particular a respiratory disease, is COVID-19, i.e., a respiratory disease, in particular pneumonia, caused by SARS-CoV-2. The resulting disease is preferably selected from the group consisting of idiopathic pulmonary hypertension, acute organ failure such as acute respiratory distress syndrome (ARDS) or acute kidney failure, pulmonary fibrosis, thrombosis, thromboembolism, blood vessel damage, blood clotting disorders, and inflammatory diseases such as PIMS (Paediatric Inflammatory Multisystem Syndrome) or Kawasaki syndrome.With regard to further features and advantages of the nucleic acid, in particular of the aforementioned protein or peptide, reference is made in full to the statements made within the scope of the first aspect of the invention to avoid repetition. The features and advantages described there with regard to the aforementioned protein or peptide also apply mutatis mutandis to the nucleic acid according to the second aspect of the invention. According to a third aspect, the invention relates to an expression vector. The expression vector comprises a nucleic acid, in particular a DNA sequence or RNA sequence, in particular an mRNA sequence, according to the second aspect of the invention. The expression vector comprises a nucleic acid, in particular a DNA sequence or RNA sequence, in particular an mRNA sequence, which encodes a protein or peptide according to the first aspect of the invention.Preferably, the nucleic acid, in particular DNA sequence or RNA sequence, in particular mRNA sequence, encodes an amino acid sequence according to sequence ID number: 11 or a variant thereof. Preferably, the variant has a sequence identity or sequence homology to the amino acid sequence according to sequence ID number: 11 of, in particular at least, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%. In particular, the expression vector may be an expression vector for use in the prophylaxis, i.e. prevention, and / or treatment of an infection and / or infectious disease caused by viruses, preferably by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof.In particular, the expression vector can be an expression vector for use in vaccination against an infection and / or infectious disease caused by coronaviruses, particularly preferably by SARS-CoV-2, and / or an infection and / or infectious disease, in particular a respiratory disease, and / or a secondary disease thereof, caused by bacteria. The infectious disease, in particular a respiratory disease, can be an acute or chronic respiratory disease. Preferably, the infectious disease, in particular a respiratory disease, is selected from the group consisting of pneumonia, acute bronchitis, the common cold, influenza, tonsillitis, laryngitis, sinusitis, bronchial asthma, chronic bronchitis, and chronic obstructive pulmonary disease (COPD). The infectious disease, in particular a respiratory disease, is preferably pneumonia.Particularly preferably, the infectious disease, in particular a respiratory disease, is viral pneumonia, i.e., a viral pneumonia, i.e., a pneumonia caused by viruses. Most preferably, the infectious disease, in particular a respiratory disease, is COVID-19, i.e., a respiratory disease, in particular pneumonia, caused by SARS-CoV-2. The resulting disease is preferably selected from the group consisting of idiopathic pulmonary hypertension, acute organ failure such as acute respiratory distress syndrome (ARDS) or acute kidney failure, pulmonary fibrosis, thrombosis, thromboembolism, blood vessel damage, blood clotting disorders, and inflammatory diseases such as PIMS (Paediatric Inflammatory Multisystem Syndrome) or Kawasaki syndrome.With regard to further features and advantages of the expression vector, in particular of the aforementioned protein or peptide and the aforementioned nucleic acid, reference is made in full to the statements made in the context of the first and second aspects of the invention to avoid repetition. The features and advantages described therein with regard to the aforementioned protein or peptide and the aforementioned nucleic acid also apply mutatis mutandis to the expression vector according to the third aspect of the invention. According to a fourth aspect, the invention relates to a host cell. The host cell contains a protein and / or peptide according to the first aspect of the invention and / or a nucleic acid, in particular a DNA sequence or RNA sequence, in particular an mRNA sequence, according to the second aspect of the invention and / or an expression vector according to the third aspect of the invention.With regard to further features and advantages of the host cell, in particular of the aforementioned protein or peptide, the aforementioned nucleic acid, and the aforementioned expression vector, reference is made in full to the statements made in the context of the first, second, and third aspects of the invention to avoid repetition. The features and advantages described there, in particular with regard to the aforementioned protein or peptide, the aforementioned nucleic acid, and the aforementioned expression vector, also apply mutatis mutandis to the host cell according to the fourth aspect of the invention. According to a fifth aspect, the invention relates to a conjugate, in particular a bioconjugate, which comprises a nanoparticle and a protein or peptide according to the first aspect of the invention or consists of a nanoparticle and a protein or peptide according to the first aspect of the invention.The conjugate according to the fifth aspect of the invention can also be referred to as a nanoparticle-protein conjugate or nanoparticle-peptide conjugate within the meaning of the present invention. The term “nanoparticle” within the meaning of the present invention is to be understood as a particle whose dimensions, in particular its diameter, preferably the mean diameter, are in a range from 1 nm to 120 nm. In this context, the term “diameter” in the case of a spherical nanoparticle is to be understood as the sphere diameter, i.e. twice the radius of the sphere. In the case of a non-spherical nanoparticle, the term “diameter” is to be understood as the greatest possible distance that two points along a circumferential line of the nanoparticle can have from one another.The use of a nanoparticle as a conjugation partner has the particular advantage that it enables the protein or peptide according to the invention and in particular optional medicinal or pharmaceutical active ingredients, in particular antivirals, to be concentrated in the body of a patient at a treatment site, for example the lungs of a patient. A further advantage is that the transport of medicinal or pharmaceutical active ingredients, in particular into the alveoli of a patient, can be facilitated by the use of a nanoparticle. A further advantage is that the conjugate according to the invention can be more easily coughed up by the nanoparticle. Preferably, the first protein or peptide segment of the protein or peptide according to the invention is centrifugally aligned or oriented on the surface of the nanoparticle, i.e. pointing away from the surface of the nanoparticle.Such alignment or orientation is particularly favored by positively charged amino acid residues contained in the protein or peptide according to the invention, in particular lysine and / or arginine residues. This results in mutual repulsion of molecules of the protein or peptide according to the invention on the surface of the nanoparticle, whereby the first protein or peptide segment of a respective protein or peptide molecule is centrifugally aligned. This prepares the amino acid sequences responsible for virus binding for ligandization with, in particular, SARS-CoV-2 particles. This advantageously optimizes virus binding and thus improves the virostatic properties of the conjugate. The conjugate preferably has a core-shell structure. The core preferably comprises the nanoparticle or preferably consists of the nanoparticle.The shell preferably comprises the protein or peptide according to the invention or preferably consists of the protein or peptide according to the invention. More preferably, the protein or peptide is linked to the nanoparticle or the surface of the nanoparticle via a linker unit. For example, the protein or peptide can be linked to the nanoparticle or the surface of the nanoparticle via a glutathione S-transferase-glutathione bond or via a SpyTag-SpyCatcher bond. With regard to further features and advantages of the linker unit, reference is made in full to the statements made in this regard within the scope of the first aspect of the invention to avoid repetition. The features and advantages described there with regard to the linker unit also apply mutatis mutandis to the conjugate according to the fifth aspect of the invention. The protein or peptide is preferably covalently linked to the nanoparticle or a surface of the nanoparticle.Alternatively or in combination, the protein or peptide can preferably be bonded non-covalently, for example by van der Waals forces, to the nanoparticle or a surface of the nanoparticle. Particularly preferably, the protein or peptide is bound to a surface of the nanoparticle by physisorption and / or chemisorption. In principle, the nanoparticle can have a cornerless shape or form, in particular spherical, oval, or elliptical, or a polyhedral shape or form, for example cube-shaped, cuboid-shaped, prism-shaped, pyramid-shaped, or spade-shaped. Furthermore, the nanoparticle can have a diameter, in particular an average diameter, of 40 nm to 120 nm, in particular 60 nm to 120 nm, preferably 80 nm to 120 nm.The diameters disclosed in this paragraph, in particular the mean diameters, have the advantage that the nanoparticle and thus the conjugate, including any virus particles bound to it, cannot be internalized into a cell, in particular a type II alveolar epithelial cell. Alternatively, the nanoparticle can have a diameter, in particular a mean diameter, of 1 nm to 40 nm, in particular 1 nm to 30 nm, preferably 5 nm to 20 nm. The diameters disclosed in this paragraph, in particular the mean diameters, enable internalization of the nanoparticle and thus of the conjugate into a cell, in particular a type II alveolar epithelial cell. Such internalization of the conjugate can be advantageous from a therapeutic point of view, depending on the nature of the nanoparticle.If the nanoparticle is a silver nanoparticle, for example, cell invasion can result in chemical changes on the surface of the silver nanoparticle, such as silver oxide radicals, which are toxic not only to the cell but also to the virus. Such intoxication advantageously only affects cells that are already particularly saturated with viruses and whose apoptosis prevents further virus replication in these cells. A noncovalent bond between the nanoparticle and the protein or peptide can advantageously further increase the toxic effect, since in this case the conjugated silver nanoparticles are exposed to increased oxidation in the intracellular space of the cell, leading to an increased release of silver oxide radicals and thus to increased apoptosis of the cell, particularly of type II alveolar epithelial cells.The nanoparticle is preferably an antimicrobially active, in particular bacteriostatic and / or virostatic, nanoparticle. For the purposes of the present invention, the term "antimicrobially active nanoparticle" is understood to mean a nanoparticle capable of reducing the replication capacity and / or infectivity of microorganisms, including viruses, or of killing or inactivating them. For the purposes of the present invention, the term "bacteriostatic nanoparticle" is understood to mean a nanoparticle capable of inhibiting the growth and / or replication of bacteria. For the purposes of the present invention, the term "virostatic nanoparticle" is understood to mean a nanoparticle capable of inhibiting the replication of viruses. The nanoparticle preferably comprises a metal or is made of metal.The metal is preferably selected from the group consisting of silver, gold, zinc, and combinations, in particular alloys, of at least two of the aforementioned metals. According to the invention, a silver or gold nanoparticle, i.e., a nanoparticle consisting of silver or gold, may be particularly preferred. The use of a silver nanoparticle generally has the advantage that it can be conjugated relatively easily with a protein or peptide. Furthermore, it is capable of cytotoxic effects (via radical formation) and thus has a virostatic effect. The use of a gold nanoparticle has the advantage that, due to its chemical inertness, it is less capable of initiating cytotoxic processes. This makes it particularly suitable, for example, for systemic, in particular intravenous, administration. Furthermore, gold nanoparticles can be provided relatively inexpensively. Furthermore, the nanoparticle can comprise a ceramic or consist of a ceramic.More preferably, the nanoparticle can comprise an organic molecule, in particular an organic carrier molecule, or consist of an organic molecule, in particular an organic carrier molecule. For the purposes of the present invention, the term "organic carrier molecule" is understood to mean an organic molecule capable of acting as a carrier for another molecule, preferably a medical or pharmaceutical active ingredient, such as, for example, an antiviral agent. For example, the organic molecule, in particular the organic carrier molecule, can be a polymer or a biomolecule, i.e., a naturally occurring molecule, such as, for example, a lipid.The organic molecule, in particular organic carrier molecule, is preferably selected from the group consisting of polysaccharides, chitosan, proteins, polyhydroxyalkanoates, polylactide, poly(lactide-co-glycolide), polyglycolide, poly-(3-hydroxybutyric acid), poly-(4-hydroxybutyric acid), polytrimethylene carbonate, poly-p-dioxanone, poly(amidoamines), lipids, polyethylene glycols and combinations, in particular mixtures, of at least two of the aforementioned organic molecules, in particular organic carrier molecules. If the organic molecule, in particular organic carrier molecule, is a protein, it may be preferred if the protein is linked directly, i.e. without a linker unit, to the protein or peptide according to the invention. More preferably, the organic molecule can form a cage, capsule or micelle structure.This is particularly advantageous from a carrier perspective, especially with regard to a medicinal or pharmaceutical active ingredient. In particular, this allows for the delayed release of, for example, a medicinal or pharmaceutical active ingredient. Furthermore, it is preferred if the conjugate comprises a medicinal or pharmaceutical active ingredient, in particular a virostatic. The medicinal or pharmaceutical active ingredient, in particular the virostatic, is preferably contained in a cage, capsule, or micelle structure of the organic molecule. This advantageously allows virucidal properties to be transferred to the conjugate. The virucidal ability of a corresponding conjugate is based in particular on the fact that, for example, virostatics can be approximated in this way to virus particles, in particular virus particles of SARS-CoV-2, which are bound to the protein or peptide according to the invention.The nanoparticle can further preferably have a coating. The nanoparticle can be at least partially, in particular only partially or completely, covered with the coating. The coating can comprise citrate and / or polyvinylpyrrolidone (PVP) or consist of citrate and / or polyvinylpyrrolidone (PVP). Particular preference is given to a silver or gold nanoparticle coated with citrate, ie a nanoparticle consisting of silver or gold that is coated with citrate. Alternatively, a silver or gold nanoparticle coated with polyvinylpyrrolidone (PVP) is preferred, ie a nanoparticle made of silver or gold that is coated with polyvinylpyrrolidone (PVP). Further preferably, the conjugate is a conjugate for use in prophylaxis, iePrevention and / or treatment of an infection and / or infectious disease caused by viruses, preferably by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof. In particular, the conjugate can be a conjugate for use in vaccination against an infection and / or infectious disease caused by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection and / or infectious disease, in particular a respiratory disease, and / or a secondary disease thereof. The infectious disease, in particular a respiratory disease, can be an acute or chronic respiratory disease.Preferably, the infectious disease, in particular a respiratory disease, is selected from the group consisting of pneumonia, acute bronchitis, colds, influenza, tonsillitis, laryngitis, sinusitis, bronchial asthma, chronic bronchitis, and chronic obstructive pulmonary disease (COPD). Preferably, the infectious disease, in particular a respiratory disease, is pneumonia. Particularly preferably, the infectious disease, in particular a respiratory disease, is viral pneumonia, i.e., a viral pneumonia, i.e., a pneumonia caused by viruses. Most preferably, the infectious disease, in particular a respiratory disease, is COVID-19, i.e., a respiratory disease, in particular pneumonia, caused by SARS-CoV-2.The secondary disease is preferably selected from the group consisting of idiopathic pulmonary hypertension, acute organ failure such as acute lung failure (ARDS, Acute Respiratory Distress Syndrome) or acute kidney failure, pulmonary fibrosis, thrombosis, thromboembolism, blood vessel damage, blood clotting disorders and inflammatory diseases such as PIMS (Paediatric Inflammatory Multisystem Syndrome) or Kawasaki syndrome. With regard to further features and advantages of the conjugate, in particular of the protein or peptide, reference is made in full to the previous description, in particular to the statements made in the context of the first aspect of the invention, in order to avoid repetition. The features and advantages described there, in particular with regard to the protein or peptide, also apply mutatis mutandis to the conjugate according to the fifth aspect of the invention. According to a sixth aspect, the invention relates to a pharmaceutical composition, i.e.a medicament or drug. The pharmaceutical composition comprises a protein or peptide according to the first aspect of the invention and / or a nucleic acid according to the second aspect of the invention and / or an expression vector according to the third aspect of the invention and / or a conjugate according to the fifth aspect of the invention. In a further embodiment of the invention, the pharmaceutical composition is prepared for inhalational administration, in particular powder inhalation, or preferably the pharmaceutical composition is used for inhalational administration, in particular powder inhalation. Inhalational administration has the advantage that, in the case of SARS-CoV-2, the target organ, the lung, can be directly addressed.In particular, it may be preferred if the pharmaceutical composition is prepared for administration in the form of an aerosol, in particular together with a propellant gas, such as carbon dioxide, nitrogen, dimethyl ether, trichlorofluoromethane, dichlorodifluoromethane, or a mixture of at least two of the aforementioned propellant gases, or is used for such administration. Such administration may be advantageous, for example, if a conjugate according to the invention is to be administered. Powder inhalation of the pharmaceutical composition may be preferred if a protein or peptide according to the invention (without conjugation with a nanoparticle) is to be administered. The human lung surface area comprises approximately 100 m. 2and is therefore very suitable for such topical application. Inhalational administration also has the advantage that it enables targeted action on the lungs, so that side effects, for example on a patient's circulatory system, are only to be expected to a limited extent, if at all. Alternatively, the pharmaceutical composition is preferably prepared for systemic, in particular intravenous, administration, or alternatively, the pharmaceutical composition is preferably used for systemic, in particular intravenous, administration. Systemic, in particular intravenous, administration advantageously allows target organs, in particular blood vessels and the heart, to be addressed. Conjugates according to the invention with gold nanoparticles, for example, are suitable for this purpose. Both blood vessels and the heart represent secondary sites of action of SARS-CoV-2.Alternatively, the pharmaceutical composition is preferably prepared for intramuscular administration or, alternatively, the pharmaceutical composition is preferably used for intramuscular administration. Alternatively, the pharmaceutical composition is preferably prepared for oral administration or, alternatively, the pharmaceutical composition is preferably used for oral administration. In the case of oral administration, the target organ can be primarily the intestine of a patient, which generally contains a virus pool. In a further embodiment of the invention, the pharmaceutical composition is a pharmaceutical composition for use in prophylaxis, iePrevention and / or treatment of an infection and / or infectious disease caused by viruses, preferably by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof. In particular, the pharmaceutical composition can be a pharmaceutical composition for use in vaccination against an infection and / or infectious disease caused by coronaviruses, particularly preferably by SARS-CoV-2, and / or a bacterial infection, in particular a respiratory disease, and / or a secondary disease thereof. The infectious disease, in particular a respiratory disease, can be an acute or chronic respiratory disease.Preferably, the infectious disease, in particular a respiratory disease, is selected from the group consisting of pneumonia, acute bronchitis, colds, influenza, tonsillitis, laryngitis, sinusitis, bronchial asthma, chronic bronchitis, and chronic obstructive pulmonary disease (COPD). Preferably, the infectious disease, in particular a respiratory disease, is pneumonia. Particularly preferably, the infectious disease, in particular a respiratory disease, is viral pneumonia, i.e., a viral pneumonia, i.e., a pneumonia caused by viruses. Most preferably, the infectious disease, in particular a respiratory disease, is COVID-19, i.e., a respiratory disease, in particular pneumonia, caused by SARS-CoV-2.The resulting disease is preferably selected from the group consisting of idiopathic pulmonary hypertension, acute organ failure such as acute respiratory distress syndrome (ARDS) or acute kidney failure, pulmonary fibrosis, thrombosis, thromboembolism, blood vessel damage, blood coagulation disorders, and inflammatory diseases such as PIMS (Paediatric Inflammatory Multisystem Syndrome) or Kawasaki syndrome. Regarding further features and advantages of the pharmaceutical composition, in particular the protein or peptide, the nucleic acid, the expression vector, and the conjugate, reference is made in full to the previous description, in particular to the statements made in the context of the first, second, third, and fifth aspects of the invention, to avoid repetition.The features and advantages described therein, in particular with regard to the protein or peptide, the nucleic acid, the expression vector, and the conjugate, also apply mutatis mutandis to the pharmaceutical composition according to the sixth aspect of the invention. According to a seventh aspect, the invention relates to a dietary supplement. The dietary supplement comprises a protein or peptide according to the first aspect of the invention and / or a nucleic acid according to the second aspect of the invention and / or an expression vector according to the third aspect of the invention and / or a conjugate according to the fifth aspect of the invention. With regard to further features and advantages of the dietary supplement, in particular the protein or peptide, the nucleic acid, the expression vector, and the conjugate, reference is made in full to the previous description, in particular to the statements made in the context of the first, second, third, and fifth aspects of the invention, to avoid repetition.The features and advantages described therein, particularly with regard to the protein or peptide, the nucleic acid, the expression vector, and the conjugate, also apply mutatis mutandis to the dietary supplement according to the seventh aspect of the invention. Further features and advantages of the invention emerge from the following description of preferred embodiments in the form of examples. Individual features can be implemented individually or in combination with one another. The preferred embodiments serve merely to further explain and improve understanding of the invention, without limiting it thereto.

[0002] EXAMPLE PART 1. Expression vector constructs: Surfactant protein D according to Sequence ID number: 1 was cloned into the expression vector pCDNA3.4 along with an MBP tag (maltose binding protein). The molecular weight of the expected protein was 35.4 kDa. The corresponding protein encoded by the construct was abbreviated "hSPD." Amino acid residues 1 to 222 of surfactant protein D, amino acid residues 19 to 90 of ACE2, and amino acid residues 223 to 375 of surfactant protein D according to Sequence ID number: 11 were cloned into the expression vector pCDNA3.4 along with an MBP tag (maltose binding protein). The molecular weight of the expected protein was 43.8 kDa. The protein encoded by the construct was designated hSPD_hACE2_insP222 2.Transfection: HEK293F cells were plated and passaged in FreeStyle 293F medium for culture growth. The day before transfection, they were cultured at a density of 2 × 106 cells / ml and fed with fresh medium. The next day, an appropriate culture volume (containing 50 × 106 cells) was centrifuged (5 min, RT, 100 × g) and the cell pellet was resuspended in 2.5 ml of fresh FreeStyle 293F medium until a final density of 20 × 106 cells / ml was achieved. The 2.5 ml cell suspension was transferred into a TubeSpin. ®Bioreactor 50. One of the expression vector constructs mentioned under 1., hSPD_hACE2_insP222 or hSPD, was added to the cell suspension at a final concentration of 30 µg / ml, and the whole mixture was mixed. Immediately afterward, 60 µg / ml of PEI MAX was added to create a stock solution of 1 mg / ml (Polyethyleneimine HCL MAX, MW 40000, cat # 24765-1, Polysciences). The culture was swirled to ensure thorough mixing of the reagents and shaken for one hour in a Minitron Infors shaker (8% CO2, 37°C, 70% humidity, 180 rpm). After one hour, 47.5 ml of previously warmed FreeStyle 293F medium was added to dilute the culture to a density of 1 x 106 cells / ml; then, the culture was transferred to a 250 ml culture flask. The cells were then allowed to grow for 96 hours (37°C, 8% CO2, 70% humidity, 125 rpm) and then harvested.Maltose 4B Agarose Purification: The culture medium (containing the secreted proteins) was harvested 96 hours after transfection (4200 rpm, 20 min, 4°C). 5 ml of 10x buffer was added to the medium and incubated for 20 minutes at 4°C. Then, 200 µl of Maltose 4B Agarose Beads (AG Scientific, # M-2795-10ML) pre-equilibrated in equilibration buffer were added, and the mixture was incubated on a rotary shaker for 2 hours at 4°C. The thickened solution was then poured onto an empty PD10 column, and the beads were washed with 10 ml of wash buffer. After washing, the bound protein was eluted with 2 x 200 µl of release buffer. After elution, the beads were boiled in 2x SDS sample buffer. All fractions were run on SDS-PAGE. The flow through each fraction was then dialyzed against 1L of 20 mM Tris-HCl pH 7.4, 150 mM NaCl, and 10 mM CaCl2 overnight at 4 °C.10x Buffer Equilibration / Wash Buffer Detachment Buffer 200mM Tris-HCl pH 20mM Tris-HCl pH 7.4 20mM Tris-HCl pH 7.4 7.4 150mM NaCl 150mM NaCl 1.5 M NaCl 10mM CaCl2 100mM EDTA 200mM CaCl2 Table 1: Buffers used and their composition The next day, 200 µl of maltose 4B agarose beads (AG Scientific, # M-2795-10 ML), which had previously been “harmonized” in equilibration buffer, were added to the dialyzed samples, and the mixture was incubated on a roller mixer at 4°C for 2 hours. The suspension was then poured onto an empty PD10 column, and the beads were washed with 10 ml of wash buffer. After washing, the bound protein was washed out or detached from the beads using 2 x 200 µl of Detachment Buffer 1 and 1 x 200 µl of Detachment Buffer 2. After washing, the beads were boiled in 2 x SDS sample buffer. All fractions were then analyzed using SDS-PAGE. Equilibration / Wash Buffer Detachment Buffer 1 Detachment Buffer 2 20 mM Tris-HCl pH 7.4 20mM Tris-HCl pH 20mM Tris-HCl pH 7.4 7.4 150mM NaCl 150mM NaCl 150mM NaCl 10mM CaCl2 50mM MnCl2 100mM EDTA Table 2: Buffers used and their composition The SDS-PAGES obtained in each case are shown photographically in Figures 1 and 2. The following is shown in the SDS-PAGE according to Fig. 1: in row 1 hSPD before dialysis, in row 2 hSPD maltose 4B agarose beads loading, in row 3 hSPD maltose 4B agarose beads flow-through, in row 4 hSPD maltose 4B agarose beads elution 1 (50 mM MnCl 2), in row 5 hSPD maltose 4B agarose beads elution 2 (50 mM MnCl 2), in row 6 hSPD maltose 4B agarose beads elution 3 (100 mM EDTA), in row 7 hSPD maltose 4B agarose boiled beads, in row 8 molecular weight markers. In the SDS-PAGE according to Fig.2 is shown: in row 1 molecular weight marker, in row 2 hSPD_hACE2_insP222 before dialysis, in row 3 hSPD_hACE2JnsP222 Maltose 4B Agarose beads loading, in row 4 hSPD_hACE2_insP222 Maltose 4B Agarose beads flow-through, in row 5 hSPD_hACE2_insP222 Maltose 4B Agarose beads elution 1 (50mM MnCl2), in row 6 hSPD_hACE2JnsP222 Maltose 4B Agarose beads elution 2 (50mM MnCl2), in row 7 hSPD_hACE2_insP222 Maltose 4B Agarose beads elution 3 (100mM EDTA), in row 8 hSPD_hACE2JnsP222 Maltose 4B Agarose Boiled beads. 4. Conclusion After transient transfection and protein expression in HEK293F cells, protein bands of the expected molecular weight were detected on SDS-PAGE in the cell supernatant samples. After dialysis of the cell culture supernatant, some of the proteins were successfully bound to the maltose beads.For both binding and detachment, several protocols described in the literature for surfactant protein D were used. The detachment fractions contained proteins with the expected molecular weights. Therefore, the corresponding bands on the gel were analyzed by mass spectrometry, and their identity was determined. For hSPD, one band was found around the expected molecular weight (slightly higher, since secreted proteins are generally glycosylated and therefore run slightly higher on the gel than the calculated molecular weight would suggest), as well as two bands with higher molecular weights. All three bands matched the human surfactant subunit D, which is described in the literature to form tightly associated higher-order oligomers. For hSPD_hACE2_insP222, only one band was detected—but not with the expected molecular weight of the oligomer.A molecular weight of 43.8 kDa was expected. Since proteins are usually glycosylated, it was not surprising that the resulting gel band corresponded to a higher molecular weight. Mass spectrometry verified the identity of the sample. The insertion of a human ACE2 sequence into hSPD thus appears to have an effect on oligomerization. The absence of oligomerization may have the advantage that the binding site of the ACE2 sequence remains freely accessible, allowing preferential binding between SARS-CoV-2 and the protein or peptide of the invention. However, this comes at the cost of reduced protein stability. The amino acid sequences mentioned in the present description correspond to the amino acid sequences disclosed in the following sequence listing.

[0003] Sequence protocol <110> Prof. Dr. med. Christoph Karle <120> Protein or peptide, in particular for the prophylaxis and / or treatment of an infection and / or infectious disease and / or a secondary disease thereof <130> P 60870 DE <160> 18 <170> BiSSAP 1.3.6 <210> 1 <211> 375 <212> PRT <213> artificial sequence <220> <223> Amino acid sequence (surfactant protein D) <400> 1 Met Leu Leu Phe Leu Leu Ser Ala Leu Val Leu Leu Thr Gln Pro Leu 1 5 10 15 Gly Tyr Leu Glu Ala Glu Met Lys Thr Tyr Ser His Arg Thr Met Pro 20 25 30 Ser Ala Cys Thr Leu Val Met Cys Ser Ser Val Glu Ser Gly Leu Pro 35 40 45 Gly Arg Asp Gly Arg Asp Gly Arg Glu Gly Pro Arg Gly Glu Lys Gly 50 55 60 Asp Pro Gly Leu Pro Gly Ala Ala Gly Gln Ala Gly Met Pro Gly Gln 65 70 75 80 Ala Gly Pro Val Gly Pro Lys Gly Asp Asn Gly Ser Val Gly Glu Pro 85 90 95 Gly Pro Lys Gly Asp Thr Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly 100 105 110 Val Pro Gly Pro Ala Gly Arg Glu Gly Pro Leu Gly Lys Gln Gly Asn 115 120 125 Ile Gly Pro Gln Gly Lys Pro Gly ProLys Gly Glu Ala Gly Pro Lys 130 135 140 Gly Glu Val Gly Ala Pro Gly Met Gln Gly Ser Ala Gly Ala Arg Gly 145 150 155 160 Leu Ala Gly Pro Lys Gly Glu Arg Gly Val Pro Gly Glu Arg Gly Val 165 170 175 Pro Gly Asn Thr Gly Ala Ala Gly Ser Ala Gly Ala Met Gly Pro Gln 180 185 190 Gly Ser Pro Gly Ala Arg Gly Pro Pro Gly Leu Lys Gly Asp Lys Gly 195 200 205 Ile Pro Gly Asp Lys Gly Ala Lys Gly Glu Ser Gly Leu Pro Asp Val 210 215 220 Ala Ser Leu Arg Gln Gln Val Glu Ala Leu Gln Gly Gln Val Gln His 225 230 235 240 Leu Gln Ala Ala Phe Ser Gln Tyr Lys Lys Val Glu Leu Phe Pro Asn 245 250 255 Gly Gln Ser Val Gly Glu Lys Ile Phe Lys Thr Ala Gly Phe Val Lys 260 265 270 Pro Phe Thr Glu Ala Gln Leu Leu Cys Thr Gln Ala Gly Gly Gln Leu 275 280 285 Ala Ser Pro Arg Ser Ala Ala Glu Asn Ala Ala Leu Gln Gln Leu Val 290 295 300 Val Ala Lys Asn Glu Ala Ala Phe Leu Ser Met Thr Asp Ser Lys Thr 305 310 315 320 Glu Gly Lys Phe Thr Tyr Pro Thr Gly Glu Ser Leu Val Tyr Ser Asn 325 330 335 Trp Ala Pro Gly Glu Pro Asn Asp AspGly Gly Ser Glu Asp Cys Val 340 345 350 Glu Ile Phe Thr Asn Gly Lys Trp Asn Asp Arg Ala Cys Gly Glu Lys 355 360 365 Arg Leu Val Val Cys Glu Phe 370 375 <210> 2 <211> 18 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste GLY205-Pro222 von Surfactant-Protein D <400> 2 Gly Asp Lys Gly Ile Pro Gly Asp Lys Gly Ala Lys Gly Glu Ser Gly 1 5 10 15 Leu Pro <210> 3 <211> 222 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste Met1-Pro222 von Surfactant-Protein D <400> 3 Met Leu Leu Phe Leu Leu Ser Ala Leu Val Leu Leu Thr Gln Pro Leu 1 5 10 15 Gly Tyr Leu Glu Ala Glu Met Lys Thr Tyr Ser His Arg Thr Met Pro 20 25 30 Ser Ala Cys Thr Leu Val Met Cys Ser Ser Val Glu Ser Gly Leu Pro 35 40 45 Gly Arg Asp Gly Arg Asp Gly Arg Glu Gly Pro Arg Gly Glu Lys Gly 50 55 60 Asp Pro Gly Leu Pro Gly Ala Ala Gly Gln Ala Gly Met Pro Gly Gln 65 70 75 80 Ala Gly Pro Val Gly Pro Lys Gly Asp Asn Gly Ser Val Gly Glu Pro 85 90 95 Gly Pro Lys Gly Asp Thr Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly 100105 110 Val Pro Gly Pro Ala Gly Arg Glu Gly Pro Leu Gly Lys Gln Gly Asn 115 120 125 Ile Gly Pro Gln Gly Lys Pro Gly Pro Lys Gly Glu Ala Gly Pro Lys 130 135 140 Gly Glu Val Gly Ala Pro Gly Met Gln Gly Ser Ala Gly Ala Arg Gly 145 150 155 160 Leu Ala Gly Pro Lys Gly Glu Arg Gly Val Pro Gly Glu Arg Gly Val 165 170 175 Pro Gly Asn Thr Gly Ala Ala Gly Ser Ala Gly Ala Met Gly Pro Gln 180 185 190 Gly Ser Pro Gly Ala Arg Gly Pro Pro Gly Leu Lys Gly Asp Lys Gly 195 200 205 Ile Pro Gly Asp Lys Gly Ala Lys Gly Glu Ser Gly Leu Pro 210 215 220 <210> 4 <211> 153 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste Asp223 bis Phe375 von Surfactant-Protein D <400> 4 Asp Val Ala Ser Leu Arg Gln Gln Val Glu Ala Leu Gln Gly Gln Val 1 5 10 15 Gln His Leu Gln Ala Ala Phe Ser Gln Tyr Lys Lys Val Glu Leu Phe 20 25 30 Pro Asn Gly Gln Ser Val Gly Glu Lys Ile Phe Lys Thr Ala Gly Phe 35 40 45 Val Lys Pro Phe Thr Glu Ala Gln Leu Leu Cys Thr Gln Ala Gly Gly 50 55 60 Gln Leu Ala Ser Pro Arg Ser Ala AlaGlu Asn Ala Ala Leu Gln Gln 65 70 75 80 Leu Val Val Ala Lys Asn Glu Ala Ala Phe Leu Ser Met Thr Asp Ser 85 90 95 Lys Thr Glu Gly Lys Phe Thr Tyr Pro Thr Gly Glu Ser Leu Val Tyr 100 105 110 Ser Asn Trp Ala Pro Gly Glu Pro Asn Asp Asp Gly Gly Ser Glu Asp 115 120 125 Cys Val Glu Ile Phe Thr Asn Gly Lys Trp Asn Asp Arg Ala Cys Gly 130 135 140 Glu Lys Arg Leu Val Val Cys Glu Phe 145 150 <210> 5 <211> 805 <212> PRT <213> artificial sequence <220> <223> Amino acid sequence (ACE2) <400> 5 Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 1 5 10 15 Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe 20 25 30 Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 35 40 45 Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 50 55 60 Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 65 70 75 80 Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 85 90 95 Leu Gln Ala Leu Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 100 105110 Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 115 120 125 Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 130 135 140 Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 145 150 155 160 Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 165 170 175 Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 180 185 190 Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu 195 200 205 Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 210 215 220 Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu 225 230 235 240 His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 245 250 255 Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 260 265 270 Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 275 280 285 Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 290 295 300 Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 305 310 315320 Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 325 330 335 Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 340 345 350 Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp 355 360 365 Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met Ala 370 375 380 Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe 385 390 395 400 His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys 405 410 415 His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn 420 425 430 Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly 435 440 445 Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe 450 455 460 Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met 465 470 475 480 Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr 485 490 495 Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe 500 505 510 Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala 515 520 525Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile 530 535 540 Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu 545 550 555 560 Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala 565 570 575 Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe 580 585 590 Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr 595 600 605 Asp Trp Ser Pro Tyr Ala Asp Gln Ser Ile Lys Val Arg Ile Ser Leu 610 615 620 Lys Ser Ala Leu Gly Asp Lys Ala Tyr Glu Trp Asn Asp Asn Glu Met 625 630 635 640 Tyr Leu Phe Arg Ser Ser Val Ala Tyr Ala Met Arg Gln Tyr Phe Leu 645 650 655 Lys Val Lys Asn Gln Met Ile Leu Phe Gly Glu Glu Asp Val Arg Val 660 665 670 Ala Asn Leu Lys Pro Arg Ile Ser Phe Asn Phe Phe Val Thr Ala Pro 675 680 685 Lys Asn Val Ser Asp Ile Ile Pro Arg Thr Glu Val Glu Lys Ala Ile 690 695 700 Arg Met Ser Arg Ser Arg Ile Asn Asp Ala Phe Arg Leu Asn Asp Asn 705 710 715 720 Ser Leu Glu Phe Leu Gly Ile Gln Pro Thr Leu Gly Pro Pro Asn Gln 725 730 735Pro Pro Val Ser Ile Trp Leu Ile Val Phe Gly Val Val Met Gly Val 740 745 750 Ile Val Val Gly Ile Val Ile Leu Ile Phe Thr Gly Ile Arg Asp Arg 755 760 765 Lys Lys Lys Asn Lys Ala Arg Ser Gly Glu Asn Pro Tyr Ala Ser Ile 770 775 780 Asp Ile Ser Lys Gly Glu Asn Asn Pro Gly Phe Gln Asn Thr Asp Asp 785 790 795 800 Val Gln Thr Ser Phe 805 <210> 6 <211> 72 <212> PRT <213> artificial sequence <220> <223> Amino acid residues Ser19-Asn90 of ACE2 <400> 6 Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn His 1 5 10 15 Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn Tyr 20 25 30 Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala Gly 35 40 45 Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln Met 50 55 60 Tyr Pro Leu Gln Glu Ile Gln Asn 65 70 <210> 7 <211> 363 <212> PRT <213> artificial sequence <220> <223> Amino acid residues 1 to 363 of ACE2 <400> 7 Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 1 5 10 15 Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys ThrPhe Leu Asp Lys Phe 20 25 30 Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 35 40 45 Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 50 55 60 Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 65 70 75 80 Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 85 90 95 Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 100 105 110 Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 115 120 125 Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 130 135 140 Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 145 150 155 160 Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 165 170 175 Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 180 185 190 Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu 195 200 205 Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 210 215 220 Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu225 230 235 240 His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 245 250 255 Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 260 265 270 Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 275 280 285 Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 290 295 300 Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 305 310 315 320 Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 325 330 335 Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 340 345 350 Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys 355 360 <210> 8 <211> 467 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste 1 bis 467 von ACE2 <400> 8 Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 1 5 10 15 Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe 20 25 30 Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 35 40 45 Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 5055 60 Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 65 70 75 80 Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 85 90 95 Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 100 105 110 Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 115 120 125 Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 130 135 140 Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 145 150 155 160 Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 165 170 175 Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 180 185 190 Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu 195 200 205 Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 210 215 220 Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu 225 230 235 240 His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 245 250 255 Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 260 265 270Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 275 280 285 Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 290 295 300 Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 305 310 315 320 Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 325 330 335 Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 340 345 350 Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp 355 360 365 Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met Ala 370 375 380 Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe 385 390 395 400 His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys 405 410 415 His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn 420 425 430 Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly 435 440 445 Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe 450 455 460 Lys Gly Glu 465 <210> 9 <211> 563 <212> PRT <213> künstliche Sequenz <220> <223>Aminosaeurereste 1 bis 563 von ACE2 <400> 9 Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 1 5 10 15 Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe 20 25 30 Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 35 40 45 Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 50 55 60 Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 65 70 75 80 Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 85 90 95 Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 100 105 110 Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 115 120 125 Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 130 135 140 Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 145 150 155 160 Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 165 170 175 Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 180 185 190 Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg GlyAsp Tyr Glu 195 200 205 Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 210 215 220 Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu 225 230 235 240 His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 245 250 255 Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 260 265 270 Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 275 280 285 Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 290 295 300 Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 305 310 315 320 Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 325 330 335 Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 340 345 350 Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp 355 360 365 Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met Ala 370 375 380 Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe 385 390 395 400 His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala AlaThr Pro Lys 405 410 415 His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn 420 425 430 Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly 435 440 445 Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val Phe 450 455 460 Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met 465 470 475 480 Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr 485 490 495 Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe 500 505 510 Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala 515 520 525 Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile 530 535 540 Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu 545 550 555 560 Gly Lys Ser <210> 10 <211> 615 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste ektope Domaene von ACE2 <400> 10 Met Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr Ala 1 5 10 15 Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe 20 25 30 Asn HisGlu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp 35 40 45 Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn 50 55 60 Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala 65 70 75 80 Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu Gln 85 90 95 Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp Lys 100 105 110 Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr Ser 115 120 125 Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu Leu 130 135 140 Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn Glu 145 150 155 160 Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln Leu 165 170 175 Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala Arg 180 185 190 Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr Glu 195 200 205 Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile Glu 210 215 220 Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His Leu 225 230 235 240 His Ala Tyr Val ArgAla Lys Leu Met Asn Ala Tyr Pro Ser Tyr Ile 245 250 255 Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp Gly 260 265 270 Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln Lys 275 280 285 Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp Ala 290 295 300 Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly Leu 305 310 315 320 Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp Pro 325 330 335 Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu Gly 340 345 350 Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp Asp 355 360 365 Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met Ala 370 375 380 Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly Phe 385 390 395 400 His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro Lys 405 410 415 His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp Asn 420 425 430 Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val Gly 435 440 445 Thr Leu Pro Phe Thr TyrMet Leu Glu Lys Trp Arg Trp Met Val Phe 450 455 460 Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu Met 465 470 475 480 Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu Thr 485 490 495 Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser Phe 500 505 510 Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu Ala 515 520 525 Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp Ile 530 535 540 Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg Leu 545 550 555 560 Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly Ala 565 570 575 Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu Phe 580 585 590 Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser Thr 595 600 605 Asp Trp Ser Pro Tyr Ala Asp 610 615 <210> 11 <211> 447 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste hSpD-ACE-hSpD <400> 11 Met Leu Leu Phe Leu Leu Ser Ala Leu Val Leu Leu Thr Gln Pro Leu 1 5 10 15 Gly Tyr Leu Glu Ala Glu Met Lys Thr TyrSer His Arg Thr Met Pro 20 25 30 Ser Ala Cys Thr Leu Val Met Cys Ser Ser Val Glu Ser Gly Leu Pro 35 40 45 Gly Arg Asp Gly Arg Asp Gly Arg Glu Gly Pro Arg Gly Glu Lys Gly 50 55 60 Asp Pro Gly Leu Pro Gly Ala Ala Gly Gln Ala Gly Met Pro Gly Gln 65 70 75 80 Ala Gly Pro Val Gly Pro Lys Gly Asp Asn Gly Ser Val Gly Glu Pro 85 90 95 Gly Pro Lys Gly Asp Thr Gly Pro Ser Gly Pro Pro Gly Pro Pro Gly 100 105 110 Val Pro Gly Pro Ala Gly Arg Glu Gly Pro Leu Gly Lys Gln Gly Asn 115 120 125 Ile Gly Pro Gln Gly Lys Pro Gly Pro Lys Gly Glu Ala Gly Pro Lys 130 135 140 Gly Glu Val Gly Ala Pro Gly Met Gln Gly Ser Ala Gly Ala Arg Gly 145 150 155 160 Leu Ala Gly Pro Lys Gly Glu Arg Gly Val Pro Gly Glu Arg Gly Val 165 170 175 Pro Gly Asn Thr Gly Ala Ala Gly Ser Ala Gly Ala Met Gly Pro Gln 180 185 190 Gly Ser Pro Gly Ala Arg Gly Pro Pro Gly Leu Lys Gly Asp Lys Gly 195 200 205 Ile Pro Gly Asp Lys Gly Ala Lys Gly Glu Ser Gly Leu Pro Ser Thr 210 215 220 Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys Phe Asn His GluAla 225 230 235 240 Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser Trp Asn Tyr Asn Thr 245 250 255 Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn Asn Ala Gly Asp Lys 260 265 270 Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu Ala Gln Met Tyr Pro 275 280 285 Leu Gln Glu Ile Gln Asn Asp Val Ala Ser Leu Arg Gln Gln Val Glu 290 295 300 Ala Leu Gln Gly Gln Val Gln His Leu Gln Ala Ala Phe Ser Gln Tyr 305 310 315 320 Lys Lys Val Glu Leu Phe Pro Asn Gly Gln Ser Val Gly Glu Lys Ile 325 330 335 Phe Lys Thr Ala Gly Phe Val Lys Pro Phe Thr Glu Ala Gln Leu Leu 340 345 350 Cys Thr Gln Ala Gly Gly Gln Leu Ala Ser Pro Arg Ser Ala Ala Glu 355 360 365 Asn Ala Ala Leu Gln Gln Leu Val Val Ala Lys Asn Glu Ala Ala Phe 370 375 380 Leu Ser Met Thr Asp Ser Lys Thr Glu Gly Lys Phe Thr Tyr Pro Thr 385 390 395 400 Gly Glu Ser Leu Val Tyr Ser Asn Trp Ala Pro Gly Glu Pro Asn Asp 405 410 415 Asp Gly Gly Ser Glu Asp Cys Val Glu Ile Phe Thr Asn Gly Lys Trp 420 425 430 Asn Asp Arg Ala Cys Gly Glu Lys Arg Leu Val Val Cys Glu Phe435 440 445 <210> 12 <211> 806 <212> PRT <213> artificial sequence <220> <223> Amino acid sequence (ACE2) <400> 12 Met Gly Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr 1 5 10 15 Ala Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys 20 25 30 Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser 35 40 45 Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn 50 55 60 Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu 65 70 75 80 Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu 85 90 95 Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp 100 105 110 Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr 115 120 125 Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu 130 135 140 Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn 145 150 155 160 Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln 165 170 175 Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu MetAla 180 185 190 Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr 195 200 205 Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile 210 215 220 Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His 225 230 235 240 Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr 245 250 255 Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp 260 265 270 Gly Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln 275 280 285 Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp 290 295 300 Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly 305 310 315 320 Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp 325 330 335 Pro Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu 340 345 350 Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp 355 360 365 Asp Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met 370 375 380 Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly385 390 395 400 Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro 405 410 415 Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp 420 425 430 Asn Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val 435 440 445 Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val 450 455 460 Phe Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu 465 470 475 480 Met Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu 485 490 495 Thr Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser 500 505 510 Phe Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu 515 520 525 Ala Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp 530 535 540 Ile Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg 545 550 555 560 Leu Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly 565 570 575 Ala Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu 580 585 590 Phe Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser595 600 605 Thr Asp Trp Ser Pro Tyr Ala Asp Gln Ser Ile Lys Val Arg Ile Ser 610 615 620 Leu Lys Ser Ala Leu Gly Asp Lys Ala Tyr Glu Trp Asn Asp Asn Glu 625 630 635 640 Met Tyr Leu Phe Arg Ser Ser Val Ala Tyr Ala Met Arg Gln Tyr Phe 645 650 655 Leu Lys Val Lys Asn Gln Met Ile Leu Phe Gly Glu Glu Asp Val Arg 660 665 670 Val Ala Asn Leu Lys Pro Arg Ile Ser Phe Asn Phe Phe Val Thr Ala 675 680 685 Pro Lys Asn Val Ser Asp Ile Ile Pro Arg Thr Glu Val Glu Lys Ala 690 695 700 Ile Arg Met Ser Arg Ser Arg Ile Asn Asp Ala Phe Arg Leu Asn Asp 705 710 715 720 Asn Ser Leu Glu Phe Leu Gly Ile Gln Pro Thr Leu Gly Pro Pro Asn 725 730 735 Gln Pro Pro Val Ser Ile Trp Leu Ile Val Phe Gly Val Val Met Gly 740 745 750 Val Ile Val Val Gly Ile Val Ile Leu Ile Phe Thr Gly Ile Arg Asp 755 760 765 Arg Lys Lys Lys Asn Lys Ala Arg Ser Gly Glu Asn Pro Tyr Ala Ser 770 775 780 Ile Asp Ile Ser Lys Gly Glu Asn Asn Pro Gly Phe Gln Asn Thr Asp 785 790 795 800 Asp Val Gln Thr Ser Phe 805 <210> 13 <211> 364 <212> PRT <213>artificial sequence <220> <223> Amino acid residues 1 to 364 of ACE2 with Gly2 <400> 13 Met Gly Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr 1 5 10 15 Ala Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys 20 25 30 Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser 35 40 45 Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn 50 55 60 Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu 65 70 75 80 Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu 85 90 95 Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp 100 105 110 Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr 115 120 125 Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu 130 135 140 Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn 145 150 155 160 Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln 165 170 175 Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala 180 185 190 Arg Ala AsnHis Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr 195 200 205 Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile 210 215 220 Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His 225 230 235 240 Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr 245 250 255 Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp 260 265 270 Gly Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln 275 280 285 Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp 290 295 300 Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly 305 310 315 320 Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp 325 330 335 Pro Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu 340 345 350 Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys 355 360 <210> 14 <211> 468 <212> PRT <213> künstliche Sequenz <220> <223> Aminosaeurereste 1 bis 468 von ACE2 mit Gly2 <400> 14 Met Gly Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr 1 510 15 Ala Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys 20 25 30 Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser 35 40 45 Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn 50 55 60 Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu 65 70 75 80 Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu 85 90 95 Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp 100 105 110 Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr 115 120 125 Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu 130 135 140 Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn 145 150 155 160 Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln 165 170 175 Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala 180 185 190 Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr 195 200 205 Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile 210 215 220 Glu Asp ValGlu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His 225 230 235 240 Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr 245 250 255 Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp 260 265 270 Gly Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln 275 280 285 Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp 290 295 300 Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly 305 310 315 320 Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp 325 330 335 Pro Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu 340 345 350 Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp 355 360 365 Asp Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met 370 375 380 Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly 385 390 395 400 Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro 405 410 415 Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp 420 425 430 Asn Glu ThrGlu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val 435 440 445 Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val 450 455 460 Phe Lys Gly Glu 465 <210> 15 <211> 564 <212> PRT <213> artificial sequence <220> <223> Amino acid residues 1 to 564 of ACE2 with Gly2 <400> 15 Met Gly Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr 1 5 10 15 Ala Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys 20 25 30 Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser 35 40 45 Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn 50 55 60 Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu 65 70 75 80 Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu 85 90 95 Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp 100 105 110 Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr 115 120 125 Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu 130 135 140 Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn SerLeu Asp Tyr Asn 145 150 155 160 Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln 165 170 175 Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala 180 185 190 Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr 195 200 205 Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile 210 215 220 Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His 225 230 235 240 Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr 245 250 255 Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp 260 265 270 Gly Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln 275 280 285 Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp 290 295 300 Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly 305 310 315 320 Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp 325 330 335 Pro Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu 340 345 350 Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr LysVal Thr Met Asp 355 360 365 Asp Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met 370 375 380 Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly 385 390 395 400 Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro 405 410 415 Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp 420 425 430 Asn Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val 435 440 445 Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val 450 455 460 Phe Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu 465 470 475 480 Met Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu 485 490 495 Thr Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser 500 505 510 Phe Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu 515 520 525 Ala Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp 530 535 540 Ile Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg 545 550 555 560 Leu Gly Lys Ser <210> 16 <211> 616 <212> PRT<213> artificial sequence <220> <223> Amino acid residues ectopic domain of ACE2 with Gly2 <400> 16 Met Gly Ser Ser Ser Ser Trp Leu Leu Leu Ser Leu Val Ala Val Thr 1 5 10 15 Ala Ala Gln Ser Thr Ile Glu Glu Gln Ala Lys Thr Phe Leu Asp Lys 20 25 30 Phe Asn His Glu Ala Glu Asp Leu Phe Tyr Gln Ser Ser Leu Ala Ser 35 40 45 Trp Asn Tyr Asn Thr Asn Ile Thr Glu Glu Asn Val Gln Asn Met Asn 50 55 60 Asn Ala Gly Asp Lys Trp Ser Ala Phe Leu Lys Glu Gln Ser Thr Leu 65 70 75 80 Ala Gln Met Tyr Pro Leu Gln Glu Ile Gln Asn Leu Thr Val Lys Leu 85 90 95 Gln Leu Gln Ala Leu Gln Gln Asn Gly Ser Ser Val Leu Ser Glu Asp 100 105 110 Lys Ser Lys Arg Leu Asn Thr Ile Leu Asn Thr Met Ser Thr Ile Tyr 115 120 125 Ser Thr Gly Lys Val Cys Asn Pro Asp Asn Pro Gln Glu Cys Leu Leu 130 135 140 Leu Glu Pro Gly Leu Asn Glu Ile Met Ala Asn Ser Leu Asp Tyr Asn 145 150 155 160 Glu Arg Leu Trp Ala Trp Glu Ser Trp Arg Ser Glu Val Gly Lys Gln 165 170 175 Leu Arg Pro Leu Tyr Glu Glu Tyr Val Val Leu Lys Asn Glu Met Ala 180 185 190Arg Ala Asn His Tyr Glu Asp Tyr Gly Asp Tyr Trp Arg Gly Asp Tyr 195 200 205 Glu Val Asn Gly Val Asp Gly Tyr Asp Tyr Ser Arg Gly Gln Leu Ile 210 215 220 Glu Asp Val Glu His Thr Phe Glu Glu Ile Lys Pro Leu Tyr Glu His 225 230 235 240 Leu His Ala Tyr Val Arg Ala Lys Leu Met Asn Ala Tyr Pro Ser Tyr 245 250 255 Ile Ser Pro Ile Gly Cys Leu Pro Ala His Leu Leu Gly Asp Met Trp 260 265 270 Gly Arg Phe Trp Thr Asn Leu Tyr Ser Leu Thr Val Pro Phe Gly Gln 275 280 285 Lys Pro Asn Ile Asp Val Thr Asp Ala Met Val Asp Gln Ala Trp Asp 290 295 300 Ala Gln Arg Ile Phe Lys Glu Ala Glu Lys Phe Phe Val Ser Val Gly 305 310 315 320 Leu Pro Asn Met Thr Gln Gly Phe Trp Glu Asn Ser Met Leu Thr Asp 325 330 335 Pro Gly Asn Val Gln Lys Ala Val Cys His Pro Thr Ala Trp Asp Leu 340 345 350 Gly Lys Gly Asp Phe Arg Ile Leu Met Cys Thr Lys Val Thr Met Asp 355 360 365 Asp Phe Leu Thr Ala His His Glu Met Gly His Ile Gln Tyr Asp Met 370 375 380 Ala Tyr Ala Ala Gln Pro Phe Leu Leu Arg Asn Gly Ala Asn Glu Gly 385 390 395 400Phe His Glu Ala Val Gly Glu Ile Met Ser Leu Ser Ala Ala Thr Pro 405 410 415 Lys His Leu Lys Ser Ile Gly Leu Leu Ser Pro Asp Phe Gln Glu Asp 420 425 430 Asn Glu Thr Glu Ile Asn Phe Leu Leu Lys Gln Ala Leu Thr Ile Val 435 440 445 Gly Thr Leu Pro Phe Thr Tyr Met Leu Glu Lys Trp Arg Trp Met Val 450 455 460 Phe Lys Gly Glu Ile Pro Lys Asp Gln Trp Met Lys Lys Trp Trp Glu 465 470 475 480 Met Lys Arg Glu Ile Val Gly Val Val Glu Pro Val Pro His Asp Glu 485 490 495 Thr Tyr Cys Asp Pro Ala Ser Leu Phe His Val Ser Asn Asp Tyr Ser 500 505 510 Phe Ile Arg Tyr Tyr Thr Arg Thr Leu Tyr Gln Phe Gln Phe Gln Glu 515 520 525 Ala Leu Cys Gln Ala Ala Lys His Glu Gly Pro Leu His Lys Cys Asp 530 535 540 Ile Ser Asn Ser Thr Glu Ala Gly Gln Lys Leu Phe Asn Met Leu Arg 545 550 555 560 Leu Gly Lys Ser Glu Pro Trp Thr Leu Ala Leu Glu Asn Val Val Gly 565 570 575 Ala Lys Asn Met Asn Val Arg Pro Leu Leu Asn Tyr Phe Glu Pro Leu 580 585 590 Phe Thr Trp Leu Lys Asp Gln Asn Lys Asn Ser Phe Val Gly Trp Ser 595 600 605 ThrAsp Trp Expensive Pro Tyr Here Asp 610 615 <210> 17 <211> 5 <212> PRT <213> artificial Sequence <220> <223> Aminosaur residues of Linker-Sequenz <400> 17 Cys Cys Cys Cys Cys 1 5 <210> 18 <211> 218 <212> PRT <213> artificial Sequence <220> <223> Aminosauresequenz Glutathion-S-Transferase <400> 18 Met Pro Met Ile Leu Gly Tyr Trp Asp Ile Arg Gly Leu Ala His Ala 1 5 10 15 Ile Arg Leu Leu Leu Glu Tyr Thr Asp Ser Ser Tyr Glu Glu Lys Lys 20 25 30 Tyr Thr Met Gly Gly Ala Pro Asp Tyr Asp Gly Tyr Trp 35 Asp 45 Glu Lys Phe Lys Leu Gly Leu Asp Phe Pro Asn Leu Pro Tyr Leu Ile 50 55 60 Asp Gly Ala His Lys Ile Thr Gln Ser Asn Ala Ile Leu Cys Tyr Ile 65 70 75 80 Ala Arg Lys His Asn Leu Cys Glu Glu Glu Glu Ar I 85 90 95 Val Asp Ile Leu Glu Asn Gln Ala Met Asp Val Ser Asn Gln Leu Ala 100 105 110 Arg Val Cys Tyr Ser Pro Asp Glu Lys Leu Lys Pro Glu Tyr Leu 130 135 140 Arg Pro Trp Phe Val Gly Asp Lys Ile ThrPhe Val Asp Phe Leu Ala 145 150 155 160 Tyr Asp Val Leu Asp Leu His Arg Ile Phe Glu Pro Asn Cys Leu Asp 165 170 175 Ala Phe Pro Asn Leu Lys Asp Phe Ile Ser Arg Phe Glu Gly 18 Ly18 Ala Glu Met Lys Ser Ser Arg Phe Leu Pro Lys Pro Leu 195 200 205 Tyr Thr Arg Met Ala Val Trp Gly Asn Lys 210 215 - - - - - - - - - - - -

Claims

Patent claims 1. Protein or peptide, comprising - a first protein or peptide segment, a second protein or peptide segment and a third protein or peptide segment, wherein - in the direction of the C-terminus of the protein or peptide, the second protein or peptide segment is arranged behind the first protein or peptide segment and the third protein or peptide segment is arranged behind the second protein or peptide segment, - the first protein or peptide segment has an amino acid sequence or consists of an amino acid sequence that corresponds to a partial sequence of a surfactant protein or a variant of a partial sequence of a surfactant protein, - the third protein or peptide segment has an amino acid sequence or consists of an amino acid sequence,which corresponds to another partial sequence of the surfactant protein or a variant of another partial sequence of the surfactant protein or a partial sequence of another surfactant protein or a variant of a partial sequence of another surfactant protein, and - the second protein or peptide segment has an amino acid sequence or consists of an amino acid sequence that corresponds to a complete amino acid sequence or a partial sequence of ACE2 or a variant of a complete amino acid sequence or a variant of a partial sequence of ACE2.

2. Protein according to claim 1, characterized in that the partial sequence of the surfactant protein is a partial sequence that begins at the N-terminus of the surfactant protein and the other partial sequence of the surfactant protein or the partial sequence of the other surfactant protein is a partial sequence,which ends at the C-terminus of the surfactant protein or the other surfactant protein.

3. Protein or peptide according to claim 1 or 2, characterized in that the partial sequence and / or other partial sequence of the surfactant protein is a complete amino acid sequence or a partial sequence of a subunit of the surfactant protein or a variant of a complete amino acid sequence or a partial sequence of a subunit of the surfactant protein and / or the partial sequence of the other surfactant protein is a complete amino acid sequence or a partial sequence of a subunit of the other surfactant protein or a variant of a complete amino acid sequence or a partial sequence of a subunit of the other surfactant protein. 4.Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the first protein or peptide segment and the amino acid sequence of the third protein or peptide segment together correspond to a complete amino acid sequence of the surfactant protein or a variant of a complete amino acid sequence of the surfactant protein.

5. Protein or peptide according to one of the preceding claims, characterized in that the surfactant protein is selected from the group consisting of surfactant protein A, surfactant protein B, surfactant protein C, surfactant protein D, and a combination of at least two of the aforementioned surfactant proteins. 6.Protein or peptide according to one of the preceding claims, characterized in that the other surfactant protein is selected from the group consisting of surfactant protein A, surfactant protein B, surfactant protein C, surfactant protein D, and a combination of at least two of the aforementioned surfactant proteins.

7. Protein or peptide according to one of the preceding claims, characterized in that the surfactant protein is surfactant protein D.

8. Protein or peptide according to one of the preceding claims, characterized in that the surfactant protein is surfactant protein D and the other surfactant protein is surfactant protein A, or vice versa.

9. Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the first protein or peptide segment and / or the amino acid sequence of the third protein or peptide segment comprise / comprises a partial sequence of an amino acid sequence according to sequence ID number: 1 or a variant of an amino acid sequence according to sequence ID number: 1 or consists of a partial sequence of an amino acid sequence according to sequence ID number: 1 or a variant of an amino acid sequence according to sequence ID number:

1. 10.Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the first protein or peptide section has an amino acid sequence of glycine, leucine, lysine, in particular starting from the N-terminus towards the C-terminus of the protein or peptide, or a variant thereof, or consists of an amino acid sequence of glycine, leucine, lysine, in particular starting from the N-terminus towards the C-terminus of the protein or peptide, or a variant thereof.

11. Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the first protein or peptide section has an amino acid sequence according to sequence ID number: 2 or a variant thereof, or consists of an amino acid sequence according to sequence ID number: 2 or a variant thereof. 12.Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the first protein or peptide section has an amino acid sequence according to sequence ID number: 3 or a variant thereof or consists of an amino acid sequence according to sequence ID number: 3 or a variant thereof.

13. Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the third protein or peptide section has an amino acid sequence according to sequence ID number: 4 or a variant thereof or consists of an amino acid sequence according to sequence ID number: 4 or a variant thereof.

14. Protein or peptide according to one of the preceding claims, characterized in that the complete amino acid sequence or the partial sequence of. ACE2 comprises the lysine located at position 31 of ACE2, the glutamate located at position 35 of ACE2, the aspartate located at position 38 of ACE2, and the methionine located at position 82 of ACE2.

15. Protein or peptide according to one of the preceding claims, characterized in that the partial sequence of ACE2 is a complete amino acid sequence or a partial sequence of an ectopic domain of ACE2, or a variant of a complete amino acid sequence or a partial sequence of an ectopic domain of ACE2. 16.Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the second protein or peptide section comprises a partial sequence of an amino acid sequence according to sequence ID number: 5 or a variant of a partial sequence of an amino acid sequence according to sequence ID number: 5 or consists of a partial sequence of an amino acid sequence according to sequence ID number: 5 or a variant of a partial sequence of an amino acid sequence according to sequence ID number:

5.

17. Protein or peptide according to claim 15, characterized in that the partial sequence is selected from the group consisting of sequence ID number: 6, sequence ID number: 7, sequence ID number: 8, sequence ID number: 9 and sequence ID number:

10. 18.Protein or peptide according to one of the preceding claims, characterized in that the amino acid sequence of the second protein or peptide section has an amino acid sequence according to sequence ID number: 6 or a variant of an amino acid sequence according to sequence ID number: 6 or consists of an amino acid sequence according to sequence ID number: 6 or a variant of an amino acid sequence according to sequence ID number:

6.

19. Protein or peptide according to one of claims 1 to 13, characterized in that the amino acid sequence of the second protein or peptide section has an amino acid sequence according to sequence ID number: 5 or a variant thereof or consists of an amino acid sequence according to sequence ID number: 5 or a variant thereof.

20. A protein or peptide according to any one of the preceding claims, characterized in that the N-terminus of the protein or peptide is the N-terminus of the first protein or peptide segment.

21. A protein or peptide according to any one of the preceding claims, characterized in that the C-terminus of the protein or peptide is the C-terminus of the third protein or peptide segment.

22. A protein or peptide according to any one of the preceding claims, characterized in that the protein or peptide has an amino acid sequence according to sequence ID number: 11 or a variant thereof or consists of an amino acid sequence according to sequence ID number: 11 or a variant thereof. 23.Nucleic acid encoding a protein or peptide according to any one of the preceding claims, expression vector comprising a nucleic acid encoding a protein or peptide according to any one of the preceding claims, or host cell containing a nucleic acid encoding a protein or peptide according to any one of the preceding claims, and / or an expression vector comprising a nucleic acid encoding a protein or peptide according to any one of the preceding claims.

24. Conjugate comprising a protein or peptide according to any one of claims 1 to 22 and a nanoparticle.

25. Pharmaceutical composition comprising a protein or peptide according to any one of claims 1 to 22 and / or a nucleic acid according to claim 23 and / or an expression vector according to claim 23 and / or a conjugate according to claim 24. 26.Pharmaceutical composition according to claim 25, characterized in that the pharmaceutical composition is prepared for an inhalation dosage form.

27. Protein or peptide according to one of claims 1 to 22, nucleic acid according to claim 23, expression vector according to claim 23, conjugate according to claim 24 or pharmaceutical composition according to claim 25 or 26 for use in the prophylaxis and / or treatment of an infection caused by viruses, in particular coronaviruses, preferably SARS-CoV. Infection and / or infectious disease caused by CoV-2 and / or bacteria, particularly respiratory disease, and / or a resulting disease. - - - - - - - - - - - - - - - -

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